(Q33935989)

30 July 2017

title

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis (English)

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30 July 2017

4

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30 July 2017

5

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30 July 2017

Jonathan C Lansing

3

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author name string

Dan McElheny

series ordinal

1

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30 July 2017

Jason R Schnell

series ordinal

2

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30 July 2017

language of work or name

English

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publication date

28 March 2005

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

30 July 2017

published in

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30 July 2017

volume

102

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30 July 2017

issue

14

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30 July 2017

page(s)

5032-5037

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

30 July 2017

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=556001

Structure, dynamics, and catalytic function of dihydrofolate reductase

5 July 2018

1 reference

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Protein conformational dynamics probed by single-molecule electron transfer.

5 July 2018

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NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis

5 July 2018

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Preorganization and protein dynamics in enzyme catalysis

5 July 2018

1 reference

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Network of coupled promoting motions in enzyme catalysis

5 July 2018

1 reference

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Enzyme dynamics during catalysis

5 July 2018

1 reference

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Slow dynamics in folded and unfolded states of an SH3 domain

5 July 2018

1 reference

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Studying excited states of proteins by NMR spectroscopy.

5 July 2018

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Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism

5 July 2018

1 reference

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Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules

5 July 2018

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Functional dynamics in the active site of the ribonuclease binase

5 July 2018

1 reference

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

5 July 2018

1 reference

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Interloop contacts modulate ligand cycling during catalysis by Escherichia coli dihydrofolate reductase

5 July 2018

1 reference

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

5 July 2018

1 reference

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

5 July 2018

1 reference

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A perspective on biological catalysis

5 July 2018

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

5 July 2018

1 reference

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Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods.

5 July 2018

1 reference

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Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=556001

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=556001

Viscosity-dependent structural fluctuations in enzyme catalysis

5 July 2018

1 reference

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Enzyme Dynamics: The Statistical Physics Approach

5 July 2018

1 reference

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Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features

5 July 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0500699102

Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0500699102

Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0500699102

Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0500699102

Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0500699102

Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0500699102

Tunneling and coupled motion in the Escherichia coli dihydrofolate reductase catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0500699102

Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization

21 January 2018

1 reference

12 December 2020

Evidence for flexibility in the function of ribonuclease A

1 reference

12 December 2020

Deletion of a highly motional residue affects formation of the Michaelis complex for Escherichia coli dihydrofolate reductase

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12 December 2020

Strength of an interloop hydrogen bond determines the kinetic pathway in catalysis by Escherichia coli dihydrofolate reductase

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12 December 2020

Identifiers

DOI

10.1073/PNAS.0500699102

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30 July 2017

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30 July 2017

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