Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering
Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-W...
Ausführliche Beschreibung
Autor*in: |
Ajito, Satoshi [verfasserIn] Hirai, Mitsuhiro [verfasserIn] Iwase, Hiroki [verfasserIn] Shimizu, Nobutaka [verfasserIn] Igarashi, Noriyuki [verfasserIn] Ohta, Noboru [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2018 |
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Schlagwörter: |
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Übergeordnetes Werk: |
Enthalten in: Physica / B - Amsterdam : Elsevier, 1988, 551, Seite 249-255 |
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Übergeordnetes Werk: |
volume:551 ; pages:249-255 |
DOI / URN: |
10.1016/j.physb.2018.03.040 |
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Katalog-ID: |
ELV001237292 |
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245 | 1 | 0 | |a Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering |
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520 | |a Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. | ||
650 | 4 | |a Myoglobin | |
650 | 4 | |a X-ray scattering | |
650 | 4 | |a Neutron scattering | |
650 | 4 | |a Trehalose | |
650 | 4 | |a Glucose | |
650 | 4 | |a Hydration | |
700 | 1 | |a Hirai, Mitsuhiro |e verfasserin |4 aut | |
700 | 1 | |a Iwase, Hiroki |e verfasserin |4 aut | |
700 | 1 | |a Shimizu, Nobutaka |e verfasserin |4 aut | |
700 | 1 | |a Igarashi, Noriyuki |e verfasserin |4 aut | |
700 | 1 | |a Ohta, Noboru |e verfasserin |4 aut | |
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allfields |
10.1016/j.physb.2018.03.040 doi (DE-627)ELV001237292 (ELSEVIER)S0921-4526(18)30241-2 DE-627 ger DE-627 rda eng 530 DE-600 33.60 bkl 51.00 bkl Ajito, Satoshi verfasserin aut Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. Myoglobin X-ray scattering Neutron scattering Trehalose Glucose Hydration Hirai, Mitsuhiro verfasserin aut Iwase, Hiroki verfasserin aut Shimizu, Nobutaka verfasserin aut Igarashi, Noriyuki verfasserin aut Ohta, Noboru verfasserin aut Enthalten in Physica / B Amsterdam : Elsevier, 1988 551, Seite 249-255 Online-Ressource (DE-627)266015093 (DE-600)1466579-7 (DE-576)074959840 1873-2135 nnns volume:551 pages:249-255 GBV_USEFLAG_U SYSFLAG_U GBV_ELV 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_63 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_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 33.60 Kondensierte Materie: Allgemeines 51.00 Werkstoffkunde: Allgemeines AR 551 249-255 |
spelling |
10.1016/j.physb.2018.03.040 doi (DE-627)ELV001237292 (ELSEVIER)S0921-4526(18)30241-2 DE-627 ger DE-627 rda eng 530 DE-600 33.60 bkl 51.00 bkl Ajito, Satoshi verfasserin aut Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. Myoglobin X-ray scattering Neutron scattering Trehalose Glucose Hydration Hirai, Mitsuhiro verfasserin aut Iwase, Hiroki verfasserin aut Shimizu, Nobutaka verfasserin aut Igarashi, Noriyuki verfasserin aut Ohta, Noboru verfasserin aut Enthalten in Physica / B Amsterdam : Elsevier, 1988 551, Seite 249-255 Online-Ressource (DE-627)266015093 (DE-600)1466579-7 (DE-576)074959840 1873-2135 nnns volume:551 pages:249-255 GBV_USEFLAG_U SYSFLAG_U GBV_ELV 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_63 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_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 33.60 Kondensierte Materie: Allgemeines 51.00 Werkstoffkunde: Allgemeines AR 551 249-255 |
allfields_unstemmed |
10.1016/j.physb.2018.03.040 doi (DE-627)ELV001237292 (ELSEVIER)S0921-4526(18)30241-2 DE-627 ger DE-627 rda eng 530 DE-600 33.60 bkl 51.00 bkl Ajito, Satoshi verfasserin aut Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. Myoglobin X-ray scattering Neutron scattering Trehalose Glucose Hydration Hirai, Mitsuhiro verfasserin aut Iwase, Hiroki verfasserin aut Shimizu, Nobutaka verfasserin aut Igarashi, Noriyuki verfasserin aut Ohta, Noboru verfasserin aut Enthalten in Physica / B Amsterdam : Elsevier, 1988 551, Seite 249-255 Online-Ressource (DE-627)266015093 (DE-600)1466579-7 (DE-576)074959840 1873-2135 nnns volume:551 pages:249-255 GBV_USEFLAG_U SYSFLAG_U GBV_ELV 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_63 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_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 33.60 Kondensierte Materie: Allgemeines 51.00 Werkstoffkunde: Allgemeines AR 551 249-255 |
allfieldsGer |
10.1016/j.physb.2018.03.040 doi (DE-627)ELV001237292 (ELSEVIER)S0921-4526(18)30241-2 DE-627 ger DE-627 rda eng 530 DE-600 33.60 bkl 51.00 bkl Ajito, Satoshi verfasserin aut Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. Myoglobin X-ray scattering Neutron scattering Trehalose Glucose Hydration Hirai, Mitsuhiro verfasserin aut Iwase, Hiroki verfasserin aut Shimizu, Nobutaka verfasserin aut Igarashi, Noriyuki verfasserin aut Ohta, Noboru verfasserin aut Enthalten in Physica / B Amsterdam : Elsevier, 1988 551, Seite 249-255 Online-Ressource (DE-627)266015093 (DE-600)1466579-7 (DE-576)074959840 1873-2135 nnns volume:551 pages:249-255 GBV_USEFLAG_U SYSFLAG_U GBV_ELV 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_63 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_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 33.60 Kondensierte Materie: Allgemeines 51.00 Werkstoffkunde: Allgemeines AR 551 249-255 |
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10.1016/j.physb.2018.03.040 doi (DE-627)ELV001237292 (ELSEVIER)S0921-4526(18)30241-2 DE-627 ger DE-627 rda eng 530 DE-600 33.60 bkl 51.00 bkl Ajito, Satoshi verfasserin aut Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering 2018 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. Myoglobin X-ray scattering Neutron scattering Trehalose Glucose Hydration Hirai, Mitsuhiro verfasserin aut Iwase, Hiroki verfasserin aut Shimizu, Nobutaka verfasserin aut Igarashi, Noriyuki verfasserin aut Ohta, Noboru verfasserin aut Enthalten in Physica / B Amsterdam : Elsevier, 1988 551, Seite 249-255 Online-Ressource (DE-627)266015093 (DE-600)1466579-7 (DE-576)074959840 1873-2135 nnns volume:551 pages:249-255 GBV_USEFLAG_U SYSFLAG_U GBV_ELV 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_63 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_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 33.60 Kondensierte Materie: Allgemeines 51.00 Werkstoffkunde: Allgemeines AR 551 249-255 |
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Ajito, Satoshi @@aut@@ Hirai, Mitsuhiro @@aut@@ Iwase, Hiroki @@aut@@ Shimizu, Nobutaka @@aut@@ Igarashi, Noriyuki @@aut@@ Ohta, Noboru @@aut@@ |
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530 DE-600 33.60 bkl 51.00 bkl Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering Myoglobin X-ray scattering Neutron scattering Trehalose Glucose Hydration |
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Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering |
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Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering |
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Ajito, Satoshi Hirai, Mitsuhiro Iwase, Hiroki Shimizu, Nobutaka Igarashi, Noriyuki Ohta, Noboru |
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title_sort |
protective action of trehalose and glucose on protein hydration shell clarified by using x-ray and neutron scattering |
title_auth |
Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering |
abstract |
Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. |
abstractGer |
Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. |
abstract_unstemmed |
Sugars are well known to retain protein structures and to protect denaturation. Protective actions of sugars on protein structures have been discussed under issues of preferential hydration and/or interaction between sugar and protein. By using synchrotron radiation wide-angle X-ray scattering (SR-WAXS) and small-angle neutron scattering (SANS) methods, we have succeeded to obtain a direct evidence of the effect of trehalose and glucose on a protein structure and hydration. Myoglobin from horse-skeletal muscles was used as one of typical globular proteins. The sugars used were trehalose and glucose whose concentrations were varied from 0% w/w to 35% w/w. The experimental SR-WAXS and SANS data combined with theoretical scattering function simulation and fitting clearly show that both sugars are preferentially excluded from the hydration-shell region of the protein to preserve hydration-shell density. up to the sugar concentration of ∼25% w/w. Compared with that of glucose (monosaccharide), the preservation action of the protein hydration-shell is much evidently seen for the case of trehalose (disaccharide), which might relate to a role of the preferential production of trehalose by organisms against extreme environmental stress. |
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title_short |
Protective action of trehalose and glucose on protein hydration shell clarified by using X-ray and neutron scattering |
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