Neutron scattering reveals the dynamic basis of protein adaptation to extreme temperature. (Q30351533)

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7 January 2020

title

Neutron scattering reveals the dynamic basis of protein adaptation to extreme temperature (English)

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7 January 2020

1

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7 January 2020

author name string

Dominique Madern

series ordinal

2

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7 January 2020

Bruno Franzetti

series ordinal

3

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7 January 2020

Giuseppe Zaccai

series ordinal

4

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7 January 2020

language of work or name

English

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publication date

3 October 2005

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Journal of Biological Chemistry

7 January 2020

published in

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7 January 2020

volume

280

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7 January 2020

issue

49

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7 January 2020

page(s)

40974-40979

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Finding and using hyperthermophilic enzymes.

7 January 2020

cites work

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Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima

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Structural equilibrium fluctuations in mesophilic and thermophilic alpha-amylase

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

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Protein flexibility from the dynamical transition: a force constant analysis

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

21 January 2018

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The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase

21 January 2018

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Protein dynamics: comparison of simulations with inelastic neutron scattering experiments

21 January 2018

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

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Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases

21 January 2018

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Molecular evolution within the L-malate and L-lactate dehydrogenase super-family

21 January 2018

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Structural stability and unfolding properties of thermostable bacterial alpha-amylases: a comparative study of homologous enzymes.

21 January 2018

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Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation

21 January 2018

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

21 January 2018

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21 January 2018

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Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases

21 January 2018

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Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3

21 January 2018

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Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect

21 January 2018

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21 January 2018

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The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum

21 January 2018

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2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability

21 January 2018

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21 January 2018

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Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M508417200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16203729%20AND%20SRC:MED&resulttype=core&format=json

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7 January 2020

Fatcat ID

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mapped directly with Wikidata item

24 November 2022

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