Interloop contacts modulate ligand cycling during catalysis by Escherichia coli dihydrofolate reductase.
about
Interaction of dihydrofolate reductase with methotrexate: ensemble and single-molecule kinetics.A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysisThe "Transport Specificity Ratio": a structure-function tool to search the protein fold for loci that control transition state stability in membrane transport catalysisDivergent evolution of protein conformational dynamics in dihydrofolate reductase.Structure and dynamics of the G121V dihydrofolate reductase mutant: lessons from a transition-state inhibitor complexEffects of a distal mutation on active site chemistry.Functionally important conformations of the Met20 loop in dihydrofolate reductase are populated by rapid thermal fluctuationsDefining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.Loop residues and catalysis in OMP synthase.Preorganization and protein dynamics in enzyme catalysis.Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase.Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis.Computational approach for ranking mutant enzymes according to catalytic reaction rates.A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.Triple isotopic labeling and kinetic isotope effects: exposing H-transfer steps in enzymatic systems.Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes.Carbon-deuterium bonds as probes of dihydrofolate reductase.Increased substrate affinity in the Escherichia coli L28R dihydrofolate reductase mutant causes trimethoprim resistance.The role of the Met20 loop in the hydride transfer in Escherichia coli dihydrofolate reductase.Selected-fit versus induced-fit protein binding: kinetic differences and mutational analysis.Conformational selection and induced changes along the catalytic cycle of Escherichia coli dihydrofolate reductase.High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP
P2860
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P2860
Interloop contacts modulate ligand cycling during catalysis by Escherichia coli dihydrofolate reductase.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Interloop contacts modulate li ...... coli dihydrofolate reductase.
@ast
Interloop contacts modulate li ...... coli dihydrofolate reductase.
@en
type
label
Interloop contacts modulate li ...... coli dihydrofolate reductase.
@ast
Interloop contacts modulate li ...... coli dihydrofolate reductase.
@en
prefLabel
Interloop contacts modulate li ...... coli dihydrofolate reductase.
@ast
Interloop contacts modulate li ...... coli dihydrofolate reductase.
@en
P2093
P356
P1433
P1476
Interloop contacts modulate li ...... coli dihydrofolate reductase.
@en
P2093
P304
P356
10.1021/BI001608N
P407
P577
2001-01-01T00:00:00Z