Roles of static and dynamic domains in stability and catalysis of adenylate kinase. (Q34478954)

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Language	Label	Description	Also known as
English	Roles of static and dynamic domains in stability and catalysis of adenylate kinase.	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Roles of static and dynamic domains in stability and catalysis of adenylate kinase. (English)

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Europe PubMed Central

PubMed publication ID

2 August 2017

author name string

Euiyoung Bae

1

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

George N Phillips

2

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

publication date

1 February 2006

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Europe PubMed Central

PubMed publication ID

2 August 2017

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

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Europe PubMed Central

PubMed publication ID

2 August 2017

103

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Europe PubMed Central

PubMed publication ID

2 August 2017

7

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Europe PubMed Central

PubMed publication ID

2 August 2017

2132-2137

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Europe PubMed Central

PubMed publication ID

2 August 2017

Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins

1 reference

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Molecular basis of cold adaptation.

1 reference

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6 July 2018

Enzyme dynamics during catalysis

1 reference

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Enzyme specificity under dynamic control II: Principal component analysis of alpha-lytic protease using global and local solvent boundary conditions

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Enzyme specificity under dynamic control: a normal mode analysis of alpha-lytic protease

1 reference

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6 July 2018

Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1413696

6 July 2018

Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1413696

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Rapid evolution of a protein in vitro by DNA shuffling

1 reference

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Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases

1 reference

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Precise gene fusion by PCR.

1 reference

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6 July 2018

Zinc, a novel structural element found in the family of bacterial adenylate kinases

1 reference

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Watching a protein as it functions with 150-ps time-resolved x-ray crystallography

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Dynamically controlled protein tunneling paths in photosynthetic reaction centers

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Calcium binding sites in tomato bushy stunt virus visualized by Laue crystallography

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

1 reference

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21 January 2018

Domain flexibility in ligand-free and inhibitor-bound Escherichia coli adenylate kinase based on a mode-coupling analysis of 15N spin relaxation

1 reference

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Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes

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21 January 2018

Evidence for increased local flexibility in psychrophilic alcohol dehydrogenase relative to its thermophilic homologue

1 reference

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21 January 2018

Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507527103

21 January 2018

Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507527103

21 January 2018

Zinc chelation and structural stability of adenylate kinase from Bacillus subtilis.

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507527103

21 January 2018

Identification of specific interactions that drive ligand-induced closure in five enzymes with classic domain movements

1 reference

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Identifying and engineering ion pairs in adenylate kinases. Insights from molecular dynamics simulations of thermophilic and mesophilic homologues

1 reference

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21 January 2018

Identifiers

10.1073/PNAS.0507527103

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

ResearchGate publication ID

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