Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaea - Wikidata - wikimedia - TriplyDB

Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaea

Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaea

http://www.wikidata.org/entity/Q33993711

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Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus Experimental evidence for the role of domain swapping in the evolution of the histone fold.Unique fluorophores in the dimeric archaeal histones hMfB and hPyA1 reveal the impact of nonnative structure in a monomeric kinetic intermediate Some like it hot: the molecular determinants of protein thermostability.Trading off stability against activity in extremophilic aldolases.Explanation of the stability of thermophilic proteins based on unique micromorphology.An appraisal of the enzyme stability-activity trade-off.

P2860

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P2860

Mutational analysis of differences in thermostability between histones from mesophilic and hyperthermophilic archaea

http://www.wikidata.org/entity/Q33993711

description

2000 nî lūn-bûn

@nan

2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

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2000年論文

@zh-hk

2000年論文

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2000年論文

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2000年论文

@wuu

name

Mutational analysis of differe ...... and hyperthermophilic archaea

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Mutational analysis of differe ...... and hyperthermophilic archaea

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type

label

Mutational analysis of differe ...... and hyperthermophilic archaea

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Mutational analysis of differe ...... and hyperthermophilic archaea

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Mutational analysis of differe ...... and hyperthermophilic archaea

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Mutational analysis of differe ...... and hyperthermophilic archaea

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JB.182.3.812-817.2000

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Journal of Bacteriology

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Mutational analysis of differe ...... and hyperthermophilic archaea

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P2093

J N Reeve

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J W Shriver

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W T Li

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P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

NMR structure of HMfB from the hyperthermophile, Methanothermus fervidus, confirms that this archaeal protein is a histone

A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme

Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima.

HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones.

The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization.

Archaeal histones, nucleosomes, and transcription initiation.

Methanobacterium formicicum, a mesophilic methanogen, contains three HFo histones.

MJ1647, an open reading frame in the genome of the hyperthermophile Methanococcus jannaschii, encodes a very thermostable archaeal histone with a C-terminal extension.

Crystallization and preliminary X-ray characterization of the Methanothermus fervidus histones HMfA and HMfB.

P304

812-817

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scholarly article

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10.1128/JB.182.3.812-817.2000

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