Dynamically achieved active site precision in enzyme catalysis
about
Dynamic behavior of rearranging carbocations - implications for terpene biosynthesisConnecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial EnzymePerturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme ActivityA dynamic Asp-Arg interaction is essential for catalysis in microsomal prostaglandin E2 synthase.The Effect of Protein Mass Modulation on Human Dihydrofolate Reductase.Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy.Substrate-Induced Carbon Monoxide Reactivity Suggests Multiple Enzyme Conformations at the Catalytic Copper M-Center of Peptidylglycine Monooxygenase.Probing reversible chemistry in coenzyme B12 -dependent ethanolamine ammonia lyase with kinetic isotope effects.Hydrostatic Pressure Studies Distinguish Global from Local Protein Motions in C-H Activation by Soybean Lipoxygenase-1.Activation of Two Sequential H-transfers in the Thymidylate Synthase Catalyzed Reaction.Examinations of the Chemical Step in Enzyme Catalysis.The role of protein dynamics in allosteric effects-introduction.Are there dynamical effects in enzyme catalysis? Some thoughts concerning the enzymatic chemical step.The general base in the thymidylate synthase catalyzed proton abstraction.Contribution of Buried Distal Amino Acid Residues in Horse Liver Alcohol Dehydrogenase to Structure and Catalysis.Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase.Free-Energy Landscape and Proton Transfer Pathways in Oxidative Deamination by Methylamine Dehydrogenase.Two Dynamical Regimes of the Substrate Radical Rearrangement Reaction in B12-Dependent Ethanolamine Ammonia-Lyase Resolve Contributions of Native Protein Configurations and Collective Configurational Fluctuations to Catalysis.Engineered control of enzyme structural dynamics and function.Controlling Proton Delivery through Catalyst Structural Dynamics.
P2860
Q26747304-9B98B076-36FF-4DCC-8ECD-0EF2E9E29D28Q27703607-9C667128-2FAE-4B1A-9310-2A4F118C5151Q36376049-82401736-B206-4C30-8E42-F543445B0FEEQ36551582-E637C848-9FE9-4702-B976-D1F3C7511860Q38619048-F3762C1E-3975-4D65-951D-8C9F3119A2BAQ38852835-D97A82C1-F6AA-4C3D-8EB1-43DA5F1656A6Q39116769-C210B61B-C37D-4966-AB05-6C011454929DQ40965673-CF2D6CE7-4434-45D2-8754-A2A43DE2A26BQ41208543-AC242649-263E-4D02-A95C-E20114C30BAEQ41873965-5916B381-780C-4494-B7E0-E0C6DF0DA95BQ41969761-26FEEA99-2B70-4A1C-A40C-A08C45180E2AQ42352746-F0B4FA80-EFBD-4B09-98BD-524FCD53D76EQ43098465-F291B566-EE2D-46E3-BEE3-F5BCE1CF87DEQ43198552-F435BDEB-0100-44B2-A634-4000165971E3Q47261759-3D3E95DC-AC86-4182-ACF5-9D40E79FA8C8Q47636214-802116F7-7997-470A-8710-806E7648DF67Q48053032-29A0FCB5-9B2F-4C86-AF7C-77760563AFFAQ48060803-93A34FB3-4217-467A-B04B-28E02D19B3F2Q49586384-A91543EA-694E-4AED-8DB7-46DBDD5DAF20Q51456369-83A17131-B435-4BD8-991C-3D493528CEA9
P2860
Dynamically achieved active site precision in enzyme catalysis
description
2015 nî lūn-bûn
@nan
2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Dynamically achieved active site precision in enzyme catalysis
@ast
Dynamically achieved active site precision in enzyme catalysis
@en
Dynamically achieved active site precision in enzyme catalysis
@nl
type
label
Dynamically achieved active site precision in enzyme catalysis
@ast
Dynamically achieved active site precision in enzyme catalysis
@en
Dynamically achieved active site precision in enzyme catalysis
@nl
prefLabel
Dynamically achieved active site precision in enzyme catalysis
@ast
Dynamically achieved active site precision in enzyme catalysis
@en
Dynamically achieved active site precision in enzyme catalysis
@nl
P2860
P356
P1476
Dynamically achieved active site precision in enzyme catalysis
@en
P2093
Judith P. Klinman
P2860
P304
P356
10.1021/AR5003347
P407
P577
2015-02-17T00:00:00Z