MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes

Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly appli...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Stiebritz, Martin T [verfasserIn]

Format:	Artikel
Sprache:	Englisch

Erschienen:	2015

Rechteinformationen:	Nutzungsrecht: © 2014 Wiley Periodicals, Inc.

Schlagwörter:	sequence‐reactivity relationship protein design metalloenzymes quantum mechanics/molecular mechanics Enzymes Quantum physics Proteins Molecular chemistry Mathematical models Chemical reactions Enzymes - chemistry Bacterial Proteins - metabolism Enzymes - metabolism Bacterial Proteins - genetics Desulfovibrio desulfuricans - metabolism Gene Expression Regulation, Bacterial - physiology Desulfovibrio desulfuricans - enzymology Metalloproteins - chemistry

Systematik:	VA 5105

Übergeordnetes Werk:	Enthalten in: Journal of computational chemistry - New York, NY : Wiley, 1980, 36(2015), 8, Seite 553-563
Übergeordnetes Werk:	volume:36 ; year:2015 ; number:8 ; pages:553-563

Links:	Volltext Link aufrufen Link aufrufen Link aufrufen

DOI / URN:	10.1002/jcc.23831

Katalog-ID:	OLC1968336338

Internformat


LEADER	01000caa a2200265 4500
001	OLC1968336338
003	DE-627
005	20220219071040.0
007	tu
008	160206s2015 xx \|\|\|\|\| 00\| \|\|eng c
024	7		\|a 10.1002/jcc.23831 \|2 doi
028	5	2	\|a PQ20160617
035			\|a (DE-627)OLC1968336338
035			\|a (DE-599)GBVOLC1968336338
035			\|a (PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03
035			\|a (KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq
040			\|a DE-627 \|b ger \|c DE-627 \|e rakwb
041			\|a eng
082	0	4	\|a 540 \|q DNB
084			\|a VA 5105 \|q AVZ \|2 rvk
084			\|a 35.05 \|2 bkl
100	1		\|a Stiebritz, Martin T \|e verfasserin \|4 aut
245	1	0	\|a MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes
264		1	\|c 2015
336			\|a Text \|b txt \|2 rdacontent
337			\|a ohne Hilfsmittel zu benutzen \|b n \|2 rdamedia
338			\|a Band \|b nc \|2 rdacarrier
520			\|a Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation.
540			\|a Nutzungsrecht: © 2014 Wiley Periodicals, Inc.
650		4	\|a sequence‐reactivity relationship
650		4	\|a protein design
650		4	\|a metalloenzymes
650		4	\|a quantum mechanics/molecular mechanics
650		4	\|a Enzymes
650		4	\|a Quantum physics
650		4	\|a Proteins
650		4	\|a Molecular chemistry
650		4	\|a Mathematical models
650		4	\|a Chemical reactions
650		4	\|a Enzymes - chemistry
650		4	\|a Bacterial Proteins - metabolism
650		4	\|a Enzymes - metabolism
650		4	\|a Bacterial Proteins - genetics
650		4	\|a Desulfovibrio desulfuricans - metabolism
650		4	\|a Gene Expression Regulation, Bacterial - physiology
650		4	\|a Desulfovibrio desulfuricans - enzymology
650		4	\|a Metalloproteins - chemistry
773	0	8	\|i Enthalten in \|t Journal of computational chemistry \|d New York, NY : Wiley, 1980 \|g 36(2015), 8, Seite 553-563 \|w (DE-627)129860301 \|w (DE-600)282917-4 \|w (DE-576)015169324 \|x 0192-8651 \|7 nnns
773	1	8	\|g volume:36 \|g year:2015 \|g number:8 \|g pages:553-563
856	4	1	\|u http://dx.doi.org/10.1002/jcc.23831 \|3 Volltext
856	4	2	\|u http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract
856	4	2	\|u http://www.ncbi.nlm.nih.gov/pubmed/25649465
856	4	2	\|u http://search.proquest.com/docview/1659818489
912			\|a GBV_USEFLAG_A
912			\|a SYSFLAG_A
912			\|a GBV_OLC
912			\|a SSG-OLC-CHE
912			\|a SSG-OLC-MAT
912			\|a SSG-OPC-MAT
912			\|a GBV_ILN_70
912			\|a GBV_ILN_4012
936	r	v	\|a VA 5105
936	b	k	\|a 35.05 \|q AVZ
951			\|a AR
952			\|d 36 \|j 2015 \|e 8 \|h 553-563

Indexfelder

author_variant	m t s mt mts
matchkey_str	article:01928651:2015----::erxpoeneinprahotexlrtoosqecratvtrl
hierarchy_sort_str	2015
bklnumber	35.05
publishDate	2015
allfields	10.1002/jcc.23831 doi PQ20160617 (DE-627)OLC1968336338 (DE-599)GBVOLC1968336338 (PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03 (KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq DE-627 ger DE-627 rakwb eng 540 DNB VA 5105 AVZ rvk 35.05 bkl Stiebritz, Martin T verfasserin aut MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation. Nutzungsrecht: © 2014 Wiley Periodicals, Inc. sequence‐reactivity relationship protein design metalloenzymes quantum mechanics/molecular mechanics Enzymes Quantum physics Proteins Molecular chemistry Mathematical models Chemical reactions Enzymes - chemistry Bacterial Proteins - metabolism Enzymes - metabolism Bacterial Proteins - genetics Desulfovibrio desulfuricans - metabolism Gene Expression Regulation, Bacterial - physiology Desulfovibrio desulfuricans - enzymology Metalloproteins - chemistry Enthalten in Journal of computational chemistry New York, NY : Wiley, 1980 36(2015), 8, Seite 553-563 (DE-627)129860301 (DE-600)282917-4 (DE-576)015169324 0192-8651 nnns volume:36 year:2015 number:8 pages:553-563 http://dx.doi.org/10.1002/jcc.23831 Volltext http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract http://www.ncbi.nlm.nih.gov/pubmed/25649465 http://search.proquest.com/docview/1659818489 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 VA 5105 35.05 AVZ AR 36 2015 8 553-563
spelling	10.1002/jcc.23831 doi PQ20160617 (DE-627)OLC1968336338 (DE-599)GBVOLC1968336338 (PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03 (KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq DE-627 ger DE-627 rakwb eng 540 DNB VA 5105 AVZ rvk 35.05 bkl Stiebritz, Martin T verfasserin aut MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation. Nutzungsrecht: © 2014 Wiley Periodicals, Inc. sequence‐reactivity relationship protein design metalloenzymes quantum mechanics/molecular mechanics Enzymes Quantum physics Proteins Molecular chemistry Mathematical models Chemical reactions Enzymes - chemistry Bacterial Proteins - metabolism Enzymes - metabolism Bacterial Proteins - genetics Desulfovibrio desulfuricans - metabolism Gene Expression Regulation, Bacterial - physiology Desulfovibrio desulfuricans - enzymology Metalloproteins - chemistry Enthalten in Journal of computational chemistry New York, NY : Wiley, 1980 36(2015), 8, Seite 553-563 (DE-627)129860301 (DE-600)282917-4 (DE-576)015169324 0192-8651 nnns volume:36 year:2015 number:8 pages:553-563 http://dx.doi.org/10.1002/jcc.23831 Volltext http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract http://www.ncbi.nlm.nih.gov/pubmed/25649465 http://search.proquest.com/docview/1659818489 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 VA 5105 35.05 AVZ AR 36 2015 8 553-563
allfields_unstemmed	10.1002/jcc.23831 doi PQ20160617 (DE-627)OLC1968336338 (DE-599)GBVOLC1968336338 (PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03 (KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq DE-627 ger DE-627 rakwb eng 540 DNB VA 5105 AVZ rvk 35.05 bkl Stiebritz, Martin T verfasserin aut MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation. Nutzungsrecht: © 2014 Wiley Periodicals, Inc. sequence‐reactivity relationship protein design metalloenzymes quantum mechanics/molecular mechanics Enzymes Quantum physics Proteins Molecular chemistry Mathematical models Chemical reactions Enzymes - chemistry Bacterial Proteins - metabolism Enzymes - metabolism Bacterial Proteins - genetics Desulfovibrio desulfuricans - metabolism Gene Expression Regulation, Bacterial - physiology Desulfovibrio desulfuricans - enzymology Metalloproteins - chemistry Enthalten in Journal of computational chemistry New York, NY : Wiley, 1980 36(2015), 8, Seite 553-563 (DE-627)129860301 (DE-600)282917-4 (DE-576)015169324 0192-8651 nnns volume:36 year:2015 number:8 pages:553-563 http://dx.doi.org/10.1002/jcc.23831 Volltext http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract http://www.ncbi.nlm.nih.gov/pubmed/25649465 http://search.proquest.com/docview/1659818489 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 VA 5105 35.05 AVZ AR 36 2015 8 553-563
allfieldsGer	10.1002/jcc.23831 doi PQ20160617 (DE-627)OLC1968336338 (DE-599)GBVOLC1968336338 (PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03 (KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq DE-627 ger DE-627 rakwb eng 540 DNB VA 5105 AVZ rvk 35.05 bkl Stiebritz, Martin T verfasserin aut MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation. Nutzungsrecht: © 2014 Wiley Periodicals, Inc. sequence‐reactivity relationship protein design metalloenzymes quantum mechanics/molecular mechanics Enzymes Quantum physics Proteins Molecular chemistry Mathematical models Chemical reactions Enzymes - chemistry Bacterial Proteins - metabolism Enzymes - metabolism Bacterial Proteins - genetics Desulfovibrio desulfuricans - metabolism Gene Expression Regulation, Bacterial - physiology Desulfovibrio desulfuricans - enzymology Metalloproteins - chemistry Enthalten in Journal of computational chemistry New York, NY : Wiley, 1980 36(2015), 8, Seite 553-563 (DE-627)129860301 (DE-600)282917-4 (DE-576)015169324 0192-8651 nnns volume:36 year:2015 number:8 pages:553-563 http://dx.doi.org/10.1002/jcc.23831 Volltext http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract http://www.ncbi.nlm.nih.gov/pubmed/25649465 http://search.proquest.com/docview/1659818489 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 VA 5105 35.05 AVZ AR 36 2015 8 553-563
allfieldsSound	10.1002/jcc.23831 doi PQ20160617 (DE-627)OLC1968336338 (DE-599)GBVOLC1968336338 (PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03 (KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq DE-627 ger DE-627 rakwb eng 540 DNB VA 5105 AVZ rvk 35.05 bkl Stiebritz, Martin T verfasserin aut MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation. Nutzungsrecht: © 2014 Wiley Periodicals, Inc. sequence‐reactivity relationship protein design metalloenzymes quantum mechanics/molecular mechanics Enzymes Quantum physics Proteins Molecular chemistry Mathematical models Chemical reactions Enzymes - chemistry Bacterial Proteins - metabolism Enzymes - metabolism Bacterial Proteins - genetics Desulfovibrio desulfuricans - metabolism Gene Expression Regulation, Bacterial - physiology Desulfovibrio desulfuricans - enzymology Metalloproteins - chemistry Enthalten in Journal of computational chemistry New York, NY : Wiley, 1980 36(2015), 8, Seite 553-563 (DE-627)129860301 (DE-600)282917-4 (DE-576)015169324 0192-8651 nnns volume:36 year:2015 number:8 pages:553-563 http://dx.doi.org/10.1002/jcc.23831 Volltext http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract http://www.ncbi.nlm.nih.gov/pubmed/25649465 http://search.proquest.com/docview/1659818489 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 VA 5105 35.05 AVZ AR 36 2015 8 553-563
language	English
source	Enthalten in Journal of computational chemistry 36(2015), 8, Seite 553-563 volume:36 year:2015 number:8 pages:553-563
sourceStr	Enthalten in Journal of computational chemistry 36(2015), 8, Seite 553-563 volume:36 year:2015 number:8 pages:553-563
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	sequence‐reactivity relationship protein design metalloenzymes quantum mechanics/molecular mechanics Enzymes Quantum physics Proteins Molecular chemistry Mathematical models Chemical reactions Enzymes - chemistry Bacterial Proteins - metabolism Enzymes - metabolism Bacterial Proteins - genetics Desulfovibrio desulfuricans - metabolism Gene Expression Regulation, Bacterial - physiology Desulfovibrio desulfuricans - enzymology Metalloproteins - chemistry
dewey-raw	540
isfreeaccess_bool	false
container_title	Journal of computational chemistry
authorswithroles_txt_mv	Stiebritz, Martin T @@aut@@
publishDateDaySort_date	2015-01-01T00:00:00Z
hierarchy_top_id	129860301
dewey-sort	3540
id	OLC1968336338
language_de	englisch
fullrecord	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1968336338</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20220219071040.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160206s2015 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1002/jcc.23831</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160617</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1968336338</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1968336338</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq</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">rakwb</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">DNB</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">VA 5105</subfield><subfield code="q">AVZ</subfield><subfield code="2">rvk</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.05</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Stiebritz, Martin T</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: © 2014 Wiley Periodicals, Inc.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">sequence‐reactivity relationship</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">protein design</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">metalloenzymes</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">quantum mechanics/molecular mechanics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enzymes</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Quantum physics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteins</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Molecular chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Mathematical models</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Chemical reactions</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enzymes - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Bacterial Proteins - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enzymes - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Bacterial Proteins - genetics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Desulfovibrio desulfuricans - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Gene Expression Regulation, Bacterial - physiology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Desulfovibrio desulfuricans - enzymology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Metalloproteins - chemistry</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Journal of computational chemistry</subfield><subfield code="d">New York, NY : Wiley, 1980</subfield><subfield code="g">36(2015), 8, Seite 553-563</subfield><subfield code="w">(DE-627)129860301</subfield><subfield code="w">(DE-600)282917-4</subfield><subfield code="w">(DE-576)015169324</subfield><subfield code="x">0192-8651</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:36</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:8</subfield><subfield code="g">pages:553-563</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1002/jcc.23831</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/25649465</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://search.proquest.com/docview/1659818489</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-MAT</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-MAT</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_4012</subfield></datafield><datafield tag="936" ind1="r" ind2="v"><subfield code="a">VA 5105</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">35.05</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">36</subfield><subfield code="j">2015</subfield><subfield code="e">8</subfield><subfield code="h">553-563</subfield></datafield></record></collection>
author	Stiebritz, Martin T
spellingShingle	Stiebritz, Martin T ddc 540 rvk VA 5105 bkl 35.05 misc sequence‐reactivity relationship misc protein design misc metalloenzymes misc quantum mechanics/molecular mechanics misc Enzymes misc Quantum physics misc Proteins misc Molecular chemistry misc Mathematical models misc Chemical reactions misc Enzymes - chemistry misc Bacterial Proteins - metabolism misc Enzymes - metabolism misc Bacterial Proteins - genetics misc Desulfovibrio desulfuricans - metabolism misc Gene Expression Regulation, Bacterial - physiology misc Desulfovibrio desulfuricans - enzymology misc Metalloproteins - chemistry MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes
authorStr	Stiebritz, Martin T
ppnlink_with_tag_str_mv	@@773@@(DE-627)129860301
format	Article
dewey-ones	540 - Chemistry & allied sciences
delete_txt_mv	keep
author_role	aut
collection	OLC
remote_str	false
illustrated	Not Illustrated
issn	0192-8651
topic_title	540 DNB VA 5105 AVZ rvk 35.05 bkl MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes sequence‐reactivity relationship protein design metalloenzymes quantum mechanics/molecular mechanics Enzymes Quantum physics Proteins Molecular chemistry Mathematical models Chemical reactions Enzymes - chemistry Bacterial Proteins - metabolism Enzymes - metabolism Bacterial Proteins - genetics Desulfovibrio desulfuricans - metabolism Gene Expression Regulation, Bacterial - physiology Desulfovibrio desulfuricans - enzymology Metalloproteins - chemistry
topic	ddc 540 rvk VA 5105 bkl 35.05 misc sequence‐reactivity relationship misc protein design misc metalloenzymes misc quantum mechanics/molecular mechanics misc Enzymes misc Quantum physics misc Proteins misc Molecular chemistry misc Mathematical models misc Chemical reactions misc Enzymes - chemistry misc Bacterial Proteins - metabolism misc Enzymes - metabolism misc Bacterial Proteins - genetics misc Desulfovibrio desulfuricans - metabolism misc Gene Expression Regulation, Bacterial - physiology misc Desulfovibrio desulfuricans - enzymology misc Metalloproteins - chemistry
topic_unstemmed	ddc 540 rvk VA 5105 bkl 35.05 misc sequence‐reactivity relationship misc protein design misc metalloenzymes misc quantum mechanics/molecular mechanics misc Enzymes misc Quantum physics misc Proteins misc Molecular chemistry misc Mathematical models misc Chemical reactions misc Enzymes - chemistry misc Bacterial Proteins - metabolism misc Enzymes - metabolism misc Bacterial Proteins - genetics misc Desulfovibrio desulfuricans - metabolism misc Gene Expression Regulation, Bacterial - physiology misc Desulfovibrio desulfuricans - enzymology misc Metalloproteins - chemistry
topic_browse	ddc 540 rvk VA 5105 bkl 35.05 misc sequence‐reactivity relationship misc protein design misc metalloenzymes misc quantum mechanics/molecular mechanics misc Enzymes misc Quantum physics misc Proteins misc Molecular chemistry misc Mathematical models misc Chemical reactions misc Enzymes - chemistry misc Bacterial Proteins - metabolism misc Enzymes - metabolism misc Bacterial Proteins - genetics misc Desulfovibrio desulfuricans - metabolism misc Gene Expression Regulation, Bacterial - physiology misc Desulfovibrio desulfuricans - enzymology misc Metalloproteins - chemistry
format_facet	Aufsätze Gedruckte Aufsätze
format_main_str_mv	Text Zeitschrift/Artikel
carriertype_str_mv	nc
hierarchy_parent_title	Journal of computational chemistry
hierarchy_parent_id	129860301
dewey-tens	540 - Chemistry
hierarchy_top_title	Journal of computational chemistry
isfreeaccess_txt	false
familylinks_str_mv	(DE-627)129860301 (DE-600)282917-4 (DE-576)015169324
title	MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes
ctrlnum	(DE-627)OLC1968336338 (DE-599)GBVOLC1968336338 (PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03 (KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq
title_full	MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes
author_sort	Stiebritz, Martin T
journal	Journal of computational chemistry
journalStr	Journal of computational chemistry
lang_code	eng
isOA_bool	false
dewey-hundreds	500 - Science
recordtype	marc
publishDateSort	2015
contenttype_str_mv	txt
container_start_page	553
author_browse	Stiebritz, Martin T
container_volume	36
class	540 DNB VA 5105 AVZ rvk 35.05 bkl
format_se	Aufsätze
author-letter	Stiebritz, Martin T
doi_str_mv	10.1002/jcc.23831
dewey-full	540
title_sort	metrex: a protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes
title_auth	MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes
abstract	Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation.
abstractGer	Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation.
abstract_unstemmed	Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012
container_issue	8
title_short	MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes
url	http://dx.doi.org/10.1002/jcc.23831 http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract http://www.ncbi.nlm.nih.gov/pubmed/25649465 http://search.proquest.com/docview/1659818489
remote_bool	false
ppnlink	129860301
mediatype_str_mv	n
isOA_txt	false
hochschulschrift_bool	false
doi_str	10.1002/jcc.23831
up_date	2024-07-04T03:07:23.218Z
_version_	1803616196475486208
fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1968336338</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20220219071040.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160206s2015 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1002/jcc.23831</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160617</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1968336338</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1968336338</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)c2371-1bf1f38576036a01814a3d858de262ab1d3ce112feb284e2b3a01dcbb88840b03</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0100255420150000036000800553metrexaproteindesignapproachfortheexplorationofseq</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">rakwb</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">DNB</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">VA 5105</subfield><subfield code="q">AVZ</subfield><subfield code="2">rvk</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">35.05</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Stiebritz, Martin T</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Metalloenzymes represent a particular challenge for any rational (re)design approach because the modeling of reaction events at their metallic cofactors requires time‐consuming quantum mechanical calculations, which cannot easily be reconciled with the fast, knowledge‐based approaches commonly applied in protein design studies. Here, an approach for the exploration of sequence‐reactivity relationships in metalloenzymes is presented (MetREx) that consists of force field‐based screening of mutants that lie energetically between a wild‐type sequence and the global minimum energy conformation and which should, therefore, be compatible with a given protein fold. Mutant candidates are subsequently evaluated with a fast and approximate quantum mechanical/molecular mechanical‐like procedure that models the influence of the protein environment on the active site by taking partial charges and van der Waals repulsions into account. The feasibility of the procedure is demonstrated for the active site of [FeFe] hydrogenase from Desulfovibrio desulfuricans . The method described allows for the identification of mutants with altered properties, such as inhibitor‐coordination energies, and the understanding of the robustness of enzymatic reaction steps with respect to variations in sequence space. © 2015 Wiley Periodicals, Inc. Investigating sequence‐reactivity relationships is crucial for understanding enzymatic activity, but can be challenging in metalloenzymes due to the complicated electronic structures of their active sites. Here, a method is presented (MetREx) that combines fast sequence screening based on protein‐design algorithms with approximate quantum mechanical/molecular mechanical property evaluation to qualitatively study how the reactivity of metallocenters is influenced by mutational variation.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: © 2014 Wiley Periodicals, Inc.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">sequence‐reactivity relationship</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">protein design</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">metalloenzymes</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">quantum mechanics/molecular mechanics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enzymes</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Quantum physics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteins</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Molecular chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Mathematical models</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Chemical reactions</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enzymes - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Bacterial Proteins - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Enzymes - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Bacterial Proteins - genetics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Desulfovibrio desulfuricans - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Gene Expression Regulation, Bacterial - physiology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Desulfovibrio desulfuricans - enzymology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Metalloproteins - chemistry</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Journal of computational chemistry</subfield><subfield code="d">New York, NY : Wiley, 1980</subfield><subfield code="g">36(2015), 8, Seite 553-563</subfield><subfield code="w">(DE-627)129860301</subfield><subfield code="w">(DE-600)282917-4</subfield><subfield code="w">(DE-576)015169324</subfield><subfield code="x">0192-8651</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:36</subfield><subfield code="g">year:2015</subfield><subfield code="g">number:8</subfield><subfield code="g">pages:553-563</subfield></datafield><datafield tag="856" ind1="4" ind2="1"><subfield code="u">http://dx.doi.org/10.1002/jcc.23831</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://onlinelibrary.wiley.com/doi/10.1002/jcc.23831/abstract</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://www.ncbi.nlm.nih.gov/pubmed/25649465</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">http://search.proquest.com/docview/1659818489</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-MAT</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-MAT</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_4012</subfield></datafield><datafield tag="936" ind1="r" ind2="v"><subfield code="a">VA 5105</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">35.05</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">36</subfield><subfield code="j">2015</subfield><subfield code="e">8</subfield><subfield code="h">553-563</subfield></datafield></record></collection>
score	7.401354

Nicht das Richtige dabei?

Schreiben Sie uns!

MetREx: A protein design approach for the exploration of sequence‐reactivity relationships in metalloenzymes

Nicht das Richtige dabei?

Zugang & Verfügbarkeit

Vorhandene Bände

Nicht das Richtige dabei?