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Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysisSecond-Contact Shell Mutation Diminishes Streptavidin–Biotin Binding Affinity through Transmitted Effects on Equilibrium DynamicsEffects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reactionChemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate ReductaseThe role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.How Accurate Are Transition States from Simulations of Enzymatic Reactions?Hydrogen tunneling links protein dynamics to enzyme catalysisCharacterizing the dynamics of functionally relevant complexes of formate dehydrogenase.Carboxyl-terminal truncations alter the activity of the human α-galactosidase ACoordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.On the relationship between thermal stability and catalytic power of enzymesDynamics and dissipation in enzyme catalysisPerturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme ActivityUnraveling the role of protein dynamics in dihydrofolate reductase catalysisA distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.Human cytidine deaminase: a biochemical characterization of its naturally occurring variants.Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Linking protein motion to enzyme catalysis.Extension and limits of the network of coupled motions correlated to hydride transfer in dihydrofolate reductase.Hydride transfer versus hydrogen radical transfer in thymidylate synthase.Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases.Network of remote and local protein dynamics in dihydrofolate reductase catalysisMicroscale synthesis and kinetic isotope effect analysis of (4R)-[Ad-(14)C, 4-(2)H] NADPH and (4R)-[Ad-(3)H,4-(2)H] NADPH.Triple isotopic labeling and kinetic isotope effects: exposing H-transfer steps in enzymatic systems.Synthesis of radiolabeled nicotinamide cofactors from labeled pyridines: versatile probes for enzyme kinetics.Hydrogen donor-acceptor fluctuations from kinetic isotope effects: a phenomenological model.Examinations of the Chemical Step in Enzyme Catalysis.Tuning of the H-transfer coordinate in primitive versus well-evolved enzymes.Examination of enzymatic H-tunneling through kinetics and dynamics.Role of Y94 in proton and hydride transfers catalyzed by thymidylate synthase.The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.Local encoding of computationally designed enzyme activity.Increased dynamic effects in a catalytically compromised variant of Escherichia coli dihydrofolate reductase.The effect of electrostatic shielding on H tunneling in R67 dihydrofolate reductase.Contribution of Buried Distal Amino Acid Residues in Horse Liver Alcohol Dehydrogenase to Structure and Catalysis.Benchmarking Quantum Mechanics/Molecular Mechanics (QM/MM) Methods on the Thymidylate Synthase-Catalyzed Hydride Transfer.Protein motions and dynamic effects in enzyme catalysis.Conformational selection and induced changes along the catalytic cycle of Escherichia coli dihydrofolate reductase.
P2860
Q27320714-CBAA8B3B-C79A-43E2-98C9-855E1835D884Q27676003-154E1F96-2933-42C6-B04E-2B65D92886F4Q28649378-DE19E74F-46A8-4C46-9428-5AC24116B418Q28830226-1EF1796D-DD06-4586-B68A-F8A6AB88B65FQ30478319-4A2A975B-95F1-4273-9435-2A53D9EDF38EQ33629992-5CBEE1BF-426E-42A7-BAAA-015E7EE2E3F9Q33792054-2D17314F-38ED-4A83-AE85-E78E011FF02BQ34241333-23E48239-6BAA-4F86-AB91-19B05CBDE7CFQ35125851-9B336FBB-8894-465C-BCD3-4D64493C848FQ35127441-28D30FC3-5317-441F-B0E2-00E2F8605C9DQ35215561-757DCF29-11B4-4F4C-9ACF-9628C04EFB24Q35239656-887102AE-5F8F-41C3-BDEB-460D3910A8F4Q36376049-0DCB8EEC-62D5-4FB3-BDF5-354BF9757BA6Q37236476-552D1E1B-110F-49BA-848C-27208A91D839Q37337246-49304795-C75D-41B9-8F4D-E115F613C026Q37523862-52A1F975-2B6D-4C87-8C23-6D235EA3260AQ38094097-7D7D29DD-3656-4BC5-BE97-91D438D1C572Q38319353-9FD3989B-713B-474B-B314-2D554C76F315Q38740550-6D82DF53-0BB5-4A1B-B6F6-86F8D45031DBQ40244989-DD3B74A7-C1F7-4CEB-9E6F-4E92544E6E17Q40351392-64091E73-68C7-40AF-9451-B2FCDA037CBEQ41361379-08375544-BDAF-420B-9B68-A36C0BDE99EBQ41553937-777DE003-8BDC-4ACC-9D4E-09A09B5ADEA2Q41868497-7D48886F-7066-4017-B7A2-4FE6763D3B81Q41905578-B32AC1DD-E325-4BB8-8B32-A1B825CDCC9CQ41907250-21389BC1-45E7-4A5C-A226-F40F93B1BE94Q41969761-26403D91-53EB-4D23-BED7-0170F77822A1Q42024471-95D82CB2-A94E-41F0-A238-77EE9A9DC7A9Q42079493-016C3432-53A8-45C0-94D7-3E7E702ECEECQ42112988-B9EAA79B-1F90-4B2C-BD52-3D7E02F45C2FQ42122813-6924F07C-D516-40D3-9237-C9C404DEE90AQ42399636-5E01BFA5-D8A2-43EA-90FE-4D5DA38AA4E1Q42414532-4A5B6B6E-AFB5-47D4-B873-D45C9341C4DEQ42911644-175A4B0A-E241-47EA-9301-D1F725EB1053Q47261759-95D4641E-E895-4030-B572-E7BE8B16DA3CQ48246521-BCA2B6FD-9614-4EEB-8EDE-A1FB2BEF565EQ53225034-C3988F59-8B4D-4E5D-BC32-581718263097Q54335575-70DE6FD1-DD62-4706-856B-FD7F5E82F3D1
P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Effects of a distal mutation on active site chemistry.
@ast
Effects of a distal mutation on active site chemistry.
@en
type
label
Effects of a distal mutation on active site chemistry.
@ast
Effects of a distal mutation on active site chemistry.
@en
prefLabel
Effects of a distal mutation on active site chemistry.
@ast
Effects of a distal mutation on active site chemistry.
@en
P2093
P2860
P356
P1433
P1476
Effects of a distal mutation on active site chemistry.
@en
P2093
Amnon Kohen
Scott Tharp
Stephen J Benkovic
Tzvia Selzer
P2860
P304
P356
10.1021/BI0518242
P407
P577
2006-02-01T00:00:00Z