Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in

Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Judy, Eva [verfasserIn] Kishore, Nand [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	Isothermal titration calorimetry Amino acids Enthalpies of interaction Desolvation enthalpy Amino acids-salt interactions

Übergeordnetes Werk:	Enthalten in: Journal of molecular structure - New York, NY [u.a.] : Elsevier, 1967, 1294
Übergeordnetes Werk:	volume:1294

DOI / URN:	10.1016/j.molstruc.2023.136401

Katalog-ID:	ELV065076249

Internformat


LEADER	01000naa a22002652 4500
001	ELV065076249
003	DE-627
005	20231011073231.0
007	cr uuu---uuuuu
008	231011s2023 xx \|\|\|\|\|o 00\| \|\|eng c
024	7		\|a 10.1016/j.molstruc.2023.136401 \|2 doi
035			\|a (DE-627)ELV065076249
035			\|a (ELSEVIER)S0022-2860(23)01491-6
040			\|a DE-627 \|b ger \|c DE-627 \|e rda
041			\|a eng
082	0	4	\|a 540 \|q VZ
084			\|a 35.00 \|2 bkl
100	1		\|a Judy, Eva \|e verfasserin \|4 aut
245	1	0	\|a Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in
264		1	\|c 2023
336			\|a nicht spezifiziert \|b zzz \|2 rdacontent
337			\|a Computermedien \|b c \|2 rdamedia
338			\|a Online-Ressource \|b cr \|2 rdacarrier
520			\|a Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction.
650		4	\|a Isothermal titration calorimetry
650		4	\|a Amino acids
650		4	\|a Enthalpies of interaction
650		4	\|a Desolvation enthalpy
650		4	\|a Amino acids-salt interactions
700	1		\|a Kishore, Nand \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Journal of molecular structure \|d New York, NY [u.a.] : Elsevier, 1967 \|g 1294 \|h Online-Ressource \|w (DE-627)302469745 \|w (DE-600)1491504-2 \|w (DE-576)255266626 \|x 0022-2860 \|7 nnns
773	1	8	\|g volume:1294
912			\|a GBV_USEFLAG_U
912			\|a GBV_ELV
912			\|a SYSFLAG_U
912			\|a SSG-OLC-PHA
912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
936	b	k	\|a 35.00 \|j Chemie: Allgemeines \|q VZ
951			\|a AR
952			\|d 1294

Indexfelder

author_variant	e j ej n k nk
matchkey_str	article:00222860:2023----::oefaesrcuapoeteiitrcinfmnaisiheainov
hierarchy_sort_str	2023
bklnumber	35.00
publishDate	2023
allfields	10.1016/j.molstruc.2023.136401 doi (DE-627)ELV065076249 (ELSEVIER)S0022-2860(23)01491-6 DE-627 ger DE-627 rda eng 540 VZ 35.00 bkl Judy, Eva verfasserin aut Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction. Isothermal titration calorimetry Amino acids Enthalpies of interaction Desolvation enthalpy Amino acids-salt interactions Kishore, Nand verfasserin aut Enthalten in Journal of molecular structure New York, NY [u.a.] : Elsevier, 1967 1294 Online-Ressource (DE-627)302469745 (DE-600)1491504-2 (DE-576)255266626 0022-2860 nnns volume:1294 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 Chemie: Allgemeines VZ AR 1294
spelling	10.1016/j.molstruc.2023.136401 doi (DE-627)ELV065076249 (ELSEVIER)S0022-2860(23)01491-6 DE-627 ger DE-627 rda eng 540 VZ 35.00 bkl Judy, Eva verfasserin aut Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction. Isothermal titration calorimetry Amino acids Enthalpies of interaction Desolvation enthalpy Amino acids-salt interactions Kishore, Nand verfasserin aut Enthalten in Journal of molecular structure New York, NY [u.a.] : Elsevier, 1967 1294 Online-Ressource (DE-627)302469745 (DE-600)1491504-2 (DE-576)255266626 0022-2860 nnns volume:1294 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 Chemie: Allgemeines VZ AR 1294
allfields_unstemmed	10.1016/j.molstruc.2023.136401 doi (DE-627)ELV065076249 (ELSEVIER)S0022-2860(23)01491-6 DE-627 ger DE-627 rda eng 540 VZ 35.00 bkl Judy, Eva verfasserin aut Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction. Isothermal titration calorimetry Amino acids Enthalpies of interaction Desolvation enthalpy Amino acids-salt interactions Kishore, Nand verfasserin aut Enthalten in Journal of molecular structure New York, NY [u.a.] : Elsevier, 1967 1294 Online-Ressource (DE-627)302469745 (DE-600)1491504-2 (DE-576)255266626 0022-2860 nnns volume:1294 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 Chemie: Allgemeines VZ AR 1294
allfieldsGer	10.1016/j.molstruc.2023.136401 doi (DE-627)ELV065076249 (ELSEVIER)S0022-2860(23)01491-6 DE-627 ger DE-627 rda eng 540 VZ 35.00 bkl Judy, Eva verfasserin aut Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction. Isothermal titration calorimetry Amino acids Enthalpies of interaction Desolvation enthalpy Amino acids-salt interactions Kishore, Nand verfasserin aut Enthalten in Journal of molecular structure New York, NY [u.a.] : Elsevier, 1967 1294 Online-Ressource (DE-627)302469745 (DE-600)1491504-2 (DE-576)255266626 0022-2860 nnns volume:1294 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 Chemie: Allgemeines VZ AR 1294
allfieldsSound	10.1016/j.molstruc.2023.136401 doi (DE-627)ELV065076249 (ELSEVIER)S0022-2860(23)01491-6 DE-627 ger DE-627 rda eng 540 VZ 35.00 bkl Judy, Eva verfasserin aut Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction. Isothermal titration calorimetry Amino acids Enthalpies of interaction Desolvation enthalpy Amino acids-salt interactions Kishore, Nand verfasserin aut Enthalten in Journal of molecular structure New York, NY [u.a.] : Elsevier, 1967 1294 Online-Ressource (DE-627)302469745 (DE-600)1491504-2 (DE-576)255266626 0022-2860 nnns volume:1294 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 Chemie: Allgemeines VZ AR 1294
language	English
source	Enthalten in Journal of molecular structure 1294 volume:1294
sourceStr	Enthalten in Journal of molecular structure 1294 volume:1294
format_phy_str_mv	Article
bklname	Chemie: Allgemeines
institution	findex.gbv.de
topic_facet	Isothermal titration calorimetry Amino acids Enthalpies of interaction Desolvation enthalpy Amino acids-salt interactions
dewey-raw	540
isfreeaccess_bool	false
container_title	Journal of molecular structure
authorswithroles_txt_mv	Judy, Eva @@aut@@ Kishore, Nand @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	302469745
dewey-sort	3540
id	ELV065076249
language_de	englisch
fullrecord	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">ELV065076249</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20231011073231.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">231011s2023 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.molstruc.2023.136401</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV065076249</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0022-2860(23)01491-6</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">540</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Judy, Eva</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2023</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Isothermal titration calorimetry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amino acids</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enthalpies of interaction</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Desolvation enthalpy</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amino acids-salt interactions</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kishore, Nand</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Journal of molecular structure</subfield><subfield code="d">New York, NY [u.a.] : Elsevier, 1967</subfield><subfield code="g">1294</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)302469745</subfield><subfield code="w">(DE-600)1491504-2</subfield><subfield code="w">(DE-576)255266626</subfield><subfield code="x">0022-2860</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:1294</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_32</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_69</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_73</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_74</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_90</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_95</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_100</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_101</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_105</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_150</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_151</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_187</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_213</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_224</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_230</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_370</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_602</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_702</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2001</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2003</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2004</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2005</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2007</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2009</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2010</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2011</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2014</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2015</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2020</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2021</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2025</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2026</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2027</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2034</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2044</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2048</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2049</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2050</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2055</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2056</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2059</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2061</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2064</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2106</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2111</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2122</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2129</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2143</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2152</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2153</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2190</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2232</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2336</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2470</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2507</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4035</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4037</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4242</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4249</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4251</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4306</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4307</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4313</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4322</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4323</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4324</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4326</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4333</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4334</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4338</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4393</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4700</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">35.00</subfield><subfield code="j">Chemie: Allgemeines</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">1294</subfield></datafield></record></collection>
author	Judy, Eva
spellingShingle	Judy, Eva ddc 540 bkl 35.00 misc Isothermal titration calorimetry misc Amino acids misc Enthalpies of interaction misc Desolvation enthalpy misc Amino acids-salt interactions Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in
authorStr	Judy, Eva
ppnlink_with_tag_str_mv	@@773@@(DE-627)302469745
format	electronic Article
dewey-ones	540 - Chemistry & allied sciences
delete_txt_mv	keep
author_role	aut aut
collection	elsevier
remote_str	true
illustrated	Not Illustrated
issn	0022-2860
topic_title	540 VZ 35.00 bkl Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in Isothermal titration calorimetry Amino acids Enthalpies of interaction Desolvation enthalpy Amino acids-salt interactions
topic	ddc 540 bkl 35.00 misc Isothermal titration calorimetry misc Amino acids misc Enthalpies of interaction misc Desolvation enthalpy misc Amino acids-salt interactions
topic_unstemmed	ddc 540 bkl 35.00 misc Isothermal titration calorimetry misc Amino acids misc Enthalpies of interaction misc Desolvation enthalpy misc Amino acids-salt interactions
topic_browse	ddc 540 bkl 35.00 misc Isothermal titration calorimetry misc Amino acids misc Enthalpies of interaction misc Desolvation enthalpy misc Amino acids-salt interactions
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
format_main_str_mv	Text Zeitschrift/Artikel
carriertype_str_mv	cr
hierarchy_parent_title	Journal of molecular structure
hierarchy_parent_id	302469745
dewey-tens	540 - Chemistry
hierarchy_top_title	Journal of molecular structure
isfreeaccess_txt	false
familylinks_str_mv	(DE-627)302469745 (DE-600)1491504-2 (DE-576)255266626
title	Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in
ctrlnum	(DE-627)ELV065076249 (ELSEVIER)S0022-2860(23)01491-6
title_full	Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in
author_sort	Judy, Eva
journal	Journal of molecular structure
journalStr	Journal of molecular structure
lang_code	eng
isOA_bool	false
dewey-hundreds	500 - Science
recordtype	marc
publishDateSort	2023
contenttype_str_mv	zzz
author_browse	Judy, Eva Kishore, Nand
container_volume	1294
class	540 VZ 35.00 bkl
format_se	Elektronische Aufsätze
author-letter	Judy, Eva
doi_str_mv	10.1016/j.molstruc.2023.136401
dewey-full	540
author2-role	verfasserin
title_sort	role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in
title_auth	Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in
abstract	Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction.
abstractGer	Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction.
abstract_unstemmed	Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction.
collection_details	GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700
title_short	Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in
remote_bool	true
author2	Kishore, Nand
author2Str	Kishore, Nand
ppnlink	302469745
mediatype_str_mv	c
isOA_txt	false
hochschulschrift_bool	false
doi_str	10.1016/j.molstruc.2023.136401
up_date	2024-07-06T21:44:46.517Z
_version_	1803867690388946944
fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">ELV065076249</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20231011073231.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">231011s2023 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.molstruc.2023.136401</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV065076249</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0022-2860(23)01491-6</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">540</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Judy, Eva</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2023</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Interactions of a homologous series of amino acids (glycine, l-alanine, DL-α-amino-n-butyric acid, l-valine and l-leucine) with salts (LiCl, NaCl, KCl, CaCl2, MnCl2, CoCl2) having common anion, but cation having varying d-electronic configuration and alkaline earth metals have been studied in aqueous solutions employing ultrasensitive isothermal titration calorimetry. Standard molar enthalpies of amino acid-salt interactions have been interpreted in terms of predominant ionic association between charged centres and the corresponding desolvation penalty. Extra crystal field stabilization experienced by M n 2 + ( a q ) and C a 2 + ( a q ) due to d 5 and d 10 electronic configuration has been addressed based on results of standard molar enthalpies of interaction. The results indicate significant desolvation cost predominantly from hydration of the cations of the salts rather than from hydration of zwitter-ionic ends of the amino acids irrespective of their chain length. This is also indicated by stronger endothermic interaction of the amino acids with the bivalent cations than that with the monovalent ones. The results obtained in this work provide essential mechanistic insights into nature of amino acid interactions modulated by variation in cationic d-electronic configuration in terms of enthalpies of interaction.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Isothermal titration calorimetry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amino acids</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enthalpies of interaction</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Desolvation enthalpy</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amino acids-salt interactions</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kishore, Nand</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Journal of molecular structure</subfield><subfield code="d">New York, NY [u.a.] : Elsevier, 1967</subfield><subfield code="g">1294</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)302469745</subfield><subfield code="w">(DE-600)1491504-2</subfield><subfield code="w">(DE-576)255266626</subfield><subfield code="x">0022-2860</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:1294</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_32</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_69</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_73</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_74</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_90</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_95</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_100</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_101</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_105</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_150</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_151</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_187</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_213</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_224</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_230</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_370</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_602</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_702</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2001</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2003</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2004</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2005</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2007</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2009</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2010</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2011</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2014</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2015</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2020</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2021</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2025</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2026</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2027</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2034</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2044</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2048</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2049</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2050</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2055</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2056</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2059</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2061</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2064</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2106</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2111</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2122</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2129</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2143</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2152</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2153</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2190</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2232</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2336</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2470</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2507</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4035</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4037</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4242</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4249</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4251</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4306</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4307</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4313</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4322</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4323</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4324</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4326</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4333</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4334</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4338</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4393</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4700</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">35.00</subfield><subfield code="j">Chemie: Allgemeines</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">1294</subfield></datafield></record></collection>
score	7.402915

Nicht das Richtige dabei?

Schreiben Sie uns!

Role of water structural properties in interaction of amino acids with metal ions of varying size and electrons in

Nicht das Richtige dabei?

Zugang & Verfügbarkeit

Vorhandene Bände

Nicht das Richtige dabei?