Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability. (Q30329248)

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Language	Label	Description	Also known as
English	Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability.	scientific article

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability. (English)

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

1

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

author name string

D Madern

2

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

C Pfister

3

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

G Zaccai

4

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

language of work or name

0 references

publication date

1 December 2001

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

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

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Europe PubMed Central

PMC publication ID

11 September 2017

98

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

25

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

14356-14361

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=64686

3 June 2018

Protein flexibility from the dynamical transition: a force constant analysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=64686

3 June 2018

Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase

1 reference

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3 June 2018

How soft is a protein? A protein dynamics force constant measured by neutron scattering.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=64686

3 June 2018

Halophilic adaptation of enzymes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=64686

3 June 2018

Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=64686

3 June 2018

Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=64686

3 June 2018

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

1 reference

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Dynamics of different functional parts of bacteriorhodopsin: H-2H labeling and neutron scattering

1 reference

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3 June 2018

Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering.

1 reference

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Charge density-dependent strength of hydration and biological structure

1 reference

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3 June 2018

Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2 M. Salt, salt concentration and temperature dependence of enzyme stabilit

1 reference

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3 June 2018

Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 1. Conformation and interaction with water and salt between 5 M and 1 M NaCl concentration

1 reference

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3 June 2018

Protein dynamics: comparison of simulations with inelastic neutron scattering experiments

1 reference

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3 June 2018

Atomic structure and chemistry of human serum albumin

1 reference

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3 June 2018

Stability of proteins: small globular proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=64686

3 June 2018

Unfolded conformations of alpha-lytic protease are more stable than its native state

1 reference

https://api.crossref.org/works/10.1073/PNAS.251537298

21 January 2018

Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions.

1 reference

https://api.crossref.org/works/10.1073/PNAS.251537298

21 January 2018

Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeo

1 reference

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21 January 2018

Correlation between drug release kinetics from proteineous matrices and protein folding: elasticity and compressibility study.

1 reference

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21 January 2018

Purification and properties of a halophilic catalase-peroxidase from Haloarcula marismortui

1 reference

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21 January 2018

How do proteins acquire their three-dimensional structure and stability?

1 reference

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26 November 2018

Microscopic origins of entropy, heat capacity and the glass transition in proteins

1 reference

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21 January 2018

A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering

1 reference

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21 January 2018

Effects of intermediates on aggregation of native bovine serum albumin

1 reference

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21 January 2018

Increased protein backbone conformational entropy upon hydrophobic ligand binding

1 reference

https://api.crossref.org/works/10.1073/PNAS.251537298

21 January 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/11734642

12 December 2020

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10.1073/PNAS.251537298

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

2001PNAS...9814356T

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

11 September 2017

ResearchGate publication ID

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