Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle.
about
A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysisThe Solution Structure of Bacillus anthracis Dihydrofolate Reductase Yields Insight into the Analysis of Structure−Activity Relationships for Novel InhibitorsNMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic InteractionsFunctional significance of evolving protein sequence in dihydrofolate reductase from bacteria to humansDivergent evolution of protein conformational dynamics in dihydrofolate reductase.Keep on moving: discovering and perturbing the conformational dynamics of enzymesStructure and dynamics of the G121V dihydrofolate reductase mutant: lessons from a transition-state inhibitor complexPreservation of protein dynamics in dihydrofolate reductase evolutionThe role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.Effects of a distal mutation on active site chemistry.Aspects of Weak Interactions between Folate and Glycine Betaine.Ligand binding and circular permutation modify residue interaction network in DHFR.Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands.Functionally important conformations of the Met20 loop in dihydrofolate reductase are populated by rapid thermal fluctuationsTemperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiencyDefining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.Taking Ockham's razor to enzyme dynamics and catalysis.Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.Molecular docking: a powerful approach for structure-based drug discoveryNeutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate.Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase.New Insights into the Role of T3 Loop in Determining Catalytic Efficiency of GH28 Endo-PolygalacturonasesMechanisms and free energies of enzymatic reactions.Multidimensional tunneling, recrossing, and the transmission coefficient for enzymatic reactionsThe mechanism of rate-limiting motions in enzyme function.Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.Interrogating the activities of conformational deformed enzyme by single-molecule fluorescence-magnetic tweezers microscopySolution structure of Archaeglobus fulgidis peptidyl-tRNA hydrolase (Pth2) provides evidence for an extensive conserved family of Pth2 enzymes in archea, bacteria, and eukaryotes.The role of large-scale motions in catalysis by dihydrofolate reductase.Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis.Connecting protein conformational dynamics with catalytic function as illustrated in dihydrofolate reductase.Role of induced fit in enzyme specificity: a molecular forward/reverse switch.A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.NMR spectroscopy brings invisible protein states into focus.Seeing the forest for the trees: fluorescence studies of single enzymes in the context of ensemble experiments.Protein dynamics and enzyme catalysis: the ghost in the machine?Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Side chain conformational averaging in human dihydrofolate reductase.The principle of conformational signaling.Protein motions during catalysis by dihydrofolate reductases.
P2860
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P2860
Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Conformational changes in the ...... se during the catalytic cycle.
@ast
Conformational changes in the ...... se during the catalytic cycle.
@en
type
label
Conformational changes in the ...... se during the catalytic cycle.
@ast
Conformational changes in the ...... se during the catalytic cycle.
@en
prefLabel
Conformational changes in the ...... se during the catalytic cycle.
@ast
Conformational changes in the ...... se during the catalytic cycle.
@en
P2093
P356
P1433
P1476
Conformational changes in the ...... ase during the catalytic cycle
@en
P2093
Dan McElheny
Eduardo Zaborowski
Rani P Venkitakrishnan
Stephen J Benkovic
P304
16046-16055
P356
10.1021/BI048119Y
P407
P577
2004-12-01T00:00:00Z