Extreme biophysics: Enzymes under pressure.

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Quasiharmonic analysis of protein energy landscapes from pressure-temperature molecular dynamics simulations.Enzymes from piezophiles.High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP

P2860

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Extreme biophysics: Enzymes under pressure.

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http://www.wikidata.org/entity/Q43029522

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2017 nî lūn-bûn

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2017年学术文章

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Extreme biophysics: Enzymes under pressure.

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Extreme biophysics: Enzymes under pressure.

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Extreme biophysics: Enzymes under pressure.

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Extreme biophysics: Enzymes under pressure.

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Extreme biophysics: Enzymes under pressure.

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Extreme biophysics: Enzymes under pressure.

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P1476

Extreme biophysics: Enzymes under pressure

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P2093

Jocelyn M Rodgers

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Qi Huang

http://www.w3.org/2001/XMLSchema#string

Russell J Hemley

http://www.w3.org/2001/XMLSchema#string

Toshiko Ichiye

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P2860

Transcriptomics reveal several gene expression patterns in the piezophile Desulfovibrio hydrothermalis in response to hydrostatic pressure

Canonical dynamics: Equilibrium phase-space distributions

The Protein Data Bank

CHARMM: the biomolecular simulation program

Cavities determine the pressure unfolding of proteins

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

All-atom empirical potential for molecular modeling and dynamics studies of proteins

Structure, dynamics, and catalytic function of dihydrofolate reductase

Development of an improved four-site water model for biomolecular simulations: TIP4P-Ew

ZINC: a free tool to discover chemistry for biology

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1174-1182

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scholarly article

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10.1002/JCC.24737

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2017-01-19T00:00:00Z

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28101963

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6334844

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Extreme biophysics: Enzymes under pressure.

about

P2860

P2860

Extreme biophysics: Enzymes under pressure.

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P1433

P1476

P2093

P2860

P304

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P2860

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