Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. - Wikidata - awgldk - TriplyDB

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

http://www.wikidata.org/entity/Q33935989

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A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis Synergistic applications of MD and NMR for the study of biological systems Structure in an extreme environment: NMR at high salt NMR and X-ray analysis of structural additivity in metal binding site-swapped hybrids of rubredoxin Solution Structure of the Squash Aspartic Acid Proteinase Inhibitor (SQAPI) and Mutational Analysis of Pepsin Inhibition Crystallographic and Nuclear Magnetic Resonance Evaluation of the Impact of Peptide Binding to the Second PDZ Domain of Protein Tyrosine Phosphatase 1E Characterization of an oxidoreductase from the arylamine N-acetyltransferase operon in Mycobacterium smegmatis Functional significance of evolving protein sequence in dihydrofolate reductase from bacteria to humans Divergent evolution of protein conformational dynamics in dihydrofolate reductase.Exploring novel strategies for AIDS protozoal pathogens: α-helix mimetics targeting a key allosteric protein–protein interaction in C. hominis thymidylate synthase-dihydrofolate reductase (TS-DHFR)Integrative, dynamic structural biology at atomic resolution--it's about time Probing the flexibility of large conformational changes in protein structures through local perturbations Histidine hydrogen-deuterium exchange mass spectrometry for probing the microenvironment of histidine residues in dihydrofolate reductase Structure and dynamics of the G121V dihydrofolate reductase mutant: lessons from a transition-state inhibitor complex Hot spots for allosteric regulation on protein surfaces Intrinsic dynamics of an enzyme underlies catalysis The role of dynamic conformational ensembles in biomolecular recognition Fluorescent biphenyl derivatives of phenylalanine suitable for protein modification.Conformational analysis of a nitroxide side chain in an α-helix with density functional theory.The 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.Ligand binding and circular permutation modify residue interaction network in DHFR.Active-site motions and polarity enhance catalytic turnover of hydrated subtilisin dissolved in organic solvents.The length of the bound fatty acid influences the dynamics of the acyl carrier protein and the stability of the thioester bond.Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands.Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.Dynamic active-site protection by the M. tuberculosis protein tyrosine phosphatase PtpB lid domain.Functionally important conformations of the Met20 loop in dihydrofolate reductase are populated by rapid thermal fluctuations Role of active site rigidity in activity: MD simulation and fluorescence study on a lipase mutant.A coevolutionary residue network at the site of a functionally important conformational change in a phosphohexomutase enzyme family.Tryptophan-based fluorophores for studying protein conformational changes.Coordinated effects of distal mutations on environmentally coupled tunneling in dihydrofolate reductase.Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate.Network of long-range concerted chemical shift displacements upon ligand binding to human angiogenin.Multiple intermediates, diverse conformations, and cooperative conformational changes underlie the catalytic hydride transfer reaction of dihydrofolate reductase.Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site.Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.Illuminating the mechanistic roles of enzyme conformational dynamics Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.The role of large-scale motions in catalysis by dihydrofolate reductase.

P2860

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P2860

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

http://www.wikidata.org/entity/Q33935989

description

2005 nî lūn-bûn

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2005 թուականի Մարտին հրատարակուած գիտական յօդուած

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2005 թվականի մարտին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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name

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

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Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

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type

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Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

@ast

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

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prefLabel

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

@ast

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.

@en

P2093

Dan McElheny

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Jason R Schnell

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P2860

Network of coupled promoting motions in enzyme catalysis

Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics

Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state

Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Structure, dynamics, and catalytic function of dihydrofolate reductase

Slow dynamics in folded and unfolded states of an SH3 domain.

Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.

Studying excited states of proteins by NMR spectroscopy.

Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle.

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5032-5037

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scholarly article

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10.1073/PNAS.0500699102

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102

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Jonathan C Lansing

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7941340

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