About: Why ion pair reversal by protein engineering is unlikely to succeed

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scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 1988 (uk) article publié dans la revue scientifique Nature (fr) নেচারে প্রকাশিত বৈজ্ঞানিক প্রবন্ধ (bn) scientific article published in Nature (en) im Juli 1988 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q57138715-82DF17EA-01AD-4FE5-9E30-B4050429DE93 wds:Q57138715-8CAF214E-EB85-4AAA-8EF1-13D1FA12E40B
publication date	1988-07-01 00:00:00Z (xsd:dateTime) 1988-07-21 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57138715-D8C14AEB-1122-4CB8-AB94-465F1C08FE02
language of work or name	English
exact match	wds:Q57138715-BE093751-B21E-4FF4-8EEA-6E8EFC52AC8F
exact match	https://scigraph.springernature.com/pub.10.1038/334270a0
cites work	wds:Q57138715-12E5818E-207D-4DF5-8087-CEDFB1A2C150 wds:Q57138715-1B66FFDF-CD2C-40C7-B12A-477B3CF50729 wds:Q57138715-2494C19E-4FAF-4D55-8DBF-BE3746FCA854 wds:Q57138715-33088106-6C58-4CF1-B630-680A1536C76E wds:Q57138715-43685BBB-C5D8-434C-AF86-2B18FE12290E wds:Q57138715-464D968D-2A8F-4751-A211-AE7612C77542 wds:Q57138715-578EADB8-FF64-489E-8C55-19B1A5F9CBC0 wds:Q57138715-5EEDA651-40B3-4ACA-AE9B-F3CF3B64ECC8 wds:Q57138715-88EBB2F6-1737-4C04-A5C8-BE89B9C3717D wds:Q57138715-94EBB9D7-E989-40C9-A772-D749C62AAB8D wds:Q57138715-A04C3A83-45E3-49FB-AA1F-542729B5A3D5 wds:Q57138715-B66A5D12-0169-409D-B4F4-7E86C5BA8AA8 wds:Q57138715-D5EDE486-AE34-41B4-99F7-4F8A9A202B85 wds:Q57138715-D676057E-3451-427E-B706-6C7F585BE086 wds:Q57138715-F8D2C8F7-18D2-4034-9048-2835B10F4C9A wds:Q57138715-FD757A94-511D-46E8-9C95-FB6A3FBB28D1
cites work	Prediction of electrostatic effects of engineering of protein charges. Calculations of enzymatic reactions: calculations of pKa, proton transfer reactions, and general acid catalysis reactions in enzymes. Calculation of electrostatic potentials in an enzyme active site Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure Free energy of charges in solvated proteins: microscopic calculations using a reversible charging process Calculations of electrostatic interactions in biological systems and in solutions Free energy perturbation calculations on binding and catalysis after mutating Asn 155 in subtilisin Energetics of enzyme catalysis Designing substrate specificity by protein engineering of electrostatic interactions Rational modification of enzyme catalysis by engineering surface charge Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin. Toward computer-aided site-directed mutagenesis of enzymes Macroscopic models for studies of electrostatic interactions in proteins: limitations and applicability Semiquantitative calculations of catalytic free energies in genetically modified enzymes Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units What about protein polarity?
author name string	wds:Q57138715-248D911D-62B4-4339-A5C1-682C3E58C3AC wds:Q57138715-61DA6738-67C1-4709-8469-FD4E892C0034
author name string	Jenn-Kang Hwang J K Hwang
rdfs:label	Why ion pair reversal by protein engineering is unlikely to succeed (en) Why ion pair reversal by protein engineering is unlikely to succeed (nl)
skos:prefLabel	Why ion pair reversal by protein engineering is unlikely to succeed (en) Why ion pair reversal by protein engineering is unlikely to succeed (nl)
name	Why ion pair reversal by protein engineering is unlikely to succeed (en) Why ion pair reversal by protein engineering is unlikely to succeed (nl)
author	wds:Q57138715-8C3168B8-CCE9-45EF-95B6-530D05125818 wds:Q57138715-C727811F-AD02-4007-8DC7-6031954CA1DF
author	Arieh Warshel
title	wds:Q57138715-3128B9DB-FD77-4D39-BE43-4A31C38CAEFE
title	Why ion pair reversal by protein engineering is unlikely to succeed (en)
page(s)	wds:Q57138715-3EA1E701-088C-40C3-9232-A6D8A2E88C5F wds:Q57138715-8C198C50-596E-4789-87F4-87A0F4D37127
page(s)	270-2 270-272
instance of	wds:Q57138715-B8EF9CC2-3C15-40E0-BF51-44F452D0E582
instance of	scholarly article
PubMed ID	wds:Q57138715-11505E50-CAE9-4B5C-87A3-C51E6CA74859
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3165161
PubMed ID	3165161
published in	wds:Q57138715-CB2EC624-7118-405D-BC43-757BEA957A67
published in	Nature
issue	wds:Q57138715-EE81C2AC-7E85-4228-A9F0-B3F11DC3B263
volume	wds:Q57138715-98205368-C448-4660-9901-DBFB6E30AAF8
issue	6179
volume	334
DOI	wds:Q57138715-65A06EBC-7B92-4852-A668-143EC66FF02F
DOI	http://dx.doi.org/10.1038/334270A0
DOI	10.1038/334270A0
Dimensions Publication ID	wds:Q57138715-244AE570-EDBB-49DC-B13A-3DF241909B5E
Dimensions Publication ID	1015697048
is owl:sameAs of	Why ion pair reversal by protein engineering is unlikely to succeed
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57138715
is cites work of	The barrier for proton transport in aquaporins as a challenge for electrostatic models: the role of protein relaxation in mutational calculations 29 Modulation of enzyme specificity by site-directed mutagenesis Comparison of in vivo selection and rational design of heterodimeric coiled coils Challenging a paradigm: theoretical calculations of the protonation state of the Cys25-His159 catalytic diad in free papain An ion pair in class II major histocompatibility complex heterodimers critical for surface expression and peptide presentation Catalysis of electron transfer during activation of O2 by the flavoprotein glucose oxidase Optimization of the electrostatic interactions between ionized groups and peptide dipoles in proteins Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations 1 1A. R. Fersht Structural basis of substrate specificity in the serine proteases Highly active and selective endopeptidases with programmed substrate specificities Engineering selectivity and discrimination into ligand-receptor interfaces Relationship between ion pair geometries and electrostatic strengths in proteins Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis Molecular dynamics study of the M412 intermediate of bacteriorhodopsin Salt bridge interactions: stability of the ionic and neutral complexes in the gas phase, in solution, and in proteins.

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