The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.
about
Effects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reactionEffects of Non-Natural Amino Acid Incorporation into the Enzyme Core Region on Enzyme Structure and Function.How Accurate Are Transition States from Simulations of Enzymatic Reactions?Hydrogen tunneling links protein dynamics to enzyme catalysisTemperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiencyCharacterizing 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.Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis.A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.Hydrogen tunneling in enzymes and biomimetic models.Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Protein motions and the activation of the CH bond catalyzed by dihydrofolate reductase.Two-dimensional infrared spectroscopy of azido-nicotinamide adenine dinucleotide in water.Computational replication of the abnormal secondary kinetic isotope effects in a hydride transfer reaction in solution with a motion assisted H-tunneling model.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.Microscale synthesis and kinetic isotope effect analysis of (4R)-[Ad-(14)C, 4-(2)H] NADPH and (4R)-[Ad-(3)H,4-(2)H] NADPH.Introduction. Biomolecular simulation.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.The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.Exploring the molecular origins of protein dynamics in the active site of human carbonic anhydrase IIThe 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.Engineered control of enzyme structural dynamics and function.Protein motions and dynamic effects in enzyme catalysis.Minimization of dynamic effects in the evolution of dihydrofolate reductase† †Electronic supplementary information (ESI) available: Full experimental procedures; mass spectra of purified proteins; circular dichroism spectra, tabulated experimental d
P2860
Q28649378-C8CEF8B8-5906-4214-B73A-D0F66B809307Q30278633-B6ADA085-D64C-4404-B419-7CB1AA90E41BQ33629992-09041174-A92C-40DA-96E2-F37CD8C584EAQ33792054-C4F330B8-F45E-4F9E-9B4F-0B947870C51AQ33933104-DB241A03-6E4D-409D-921A-F8AC3AD3876AQ34241333-1DB6DF6D-C91A-46E6-AB6E-764AE54F373BQ35125851-9C63BD5A-8ACF-459E-AED9-E370D59FC46AQ35127441-7243A054-848A-4C6C-8C9B-6D44F4AF888AQ36924776-5ED46C02-FD90-4257-80ED-E9088AA7B016Q37337246-27497785-BCE8-4240-BDAF-BEAA67F63479Q37695037-559F822F-A307-41D5-B706-52491BE1495EQ38094097-F92ECA72-8AF7-48A6-8601-36F4A3970B5BQ38205312-E5906442-C4F9-4D60-9E75-78DF5189B3BFQ38264781-4E460DAB-F6EE-47F0-A5AE-47F0FCA44BCDQ38740375-6358EB47-FA5C-40E0-9704-3EC6562692EFQ38740550-B60AD430-7C53-4B1F-BB0E-0923F0EF0B46Q40244989-08C4104B-14C0-49E9-B915-075F87F331C8Q41553937-B1801920-BC67-4451-93FC-C72EFC6E260DQ41899666-7E5A3A47-9A35-42F8-B10C-0A38AD3A1678Q41907250-5615A544-02A4-4D30-B84D-5240F41A68AEQ41969761-125D2E28-40F8-47DB-B8CB-E50C7C054B00Q42024471-9EB13245-1222-4052-8A59-6E04BBE5E4D4Q42122813-1DC93A0C-93DF-41E9-B953-FDB41922D41DQ42542577-1A5D6537-32EF-4F96-8568-FF5B257A5EC0Q42911644-A1C0E40F-D5C5-42E1-B004-AC275CB816FFQ47261759-FC8B4F4E-352B-47BC-B13E-DF241194AF24Q49586384-A5A2B558-EA92-4078-B36F-C6B4C3611F74Q53225034-21C62AF3-36B1-4C01-B8CF-5F5E2A9C2828Q55532983-A8B4C7BD-A86A-4CD4-9EEC-8E911C0553B1
P2860
The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին 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
The role of enzyme dynamics an ...... ts of dihydrofolate reductase.
@ast
The role of enzyme dynamics an ...... ts of dihydrofolate reductase.
@en
type
label
The role of enzyme dynamics an ...... ts of dihydrofolate reductase.
@ast
The role of enzyme dynamics an ...... ts of dihydrofolate reductase.
@en
prefLabel
The role of enzyme dynamics an ...... ts of dihydrofolate reductase.
@ast
The role of enzyme dynamics an ...... ts of dihydrofolate reductase.
@en
P2093
P2860
P356
P1476
The role of enzyme dynamics an ...... ts of dihydrofolate reductase.
@en
P2093
Amnon Kohen
Nina M Goodey
Stephen J Benkovic
P2860
P304
P356
10.1098/RSTB.2006.1871
P407
P577
2006-08-01T00:00:00Z