Pressure-induced structural transition of mature HIV-1 protease from a combined NMR/MD simulation approach.

Roche, Julien; Louis, John M; Bax, Ad; Best, Robert B

Roche, Julien; Louis, John M; Bax, Ad; Best, Robert B.

Afiliação

Roche J; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, 20892.
Louis JM; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, 20892.
Bax A; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, 20892.
Best RB; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, 20892.

Proteins ; 83(12): 2117-23, 2015 Dec.

Article em En | MEDLINE | ID: mdl-26385843

Assuntos

Protease de HIV/química; Protease de HIV/genética; Protease de HIV/metabolismo; Inibidores da Protease de HIV/química; Inibidores da Protease de HIV/farmacologia; Espectroscopia de Ressonância Magnética; Modelos Moleculares; Simulação de Dinâmica Molecular; Mutação; Pressão; Conformação Proteica

Palavras-chave

cavities; conformational fluctuations; high-pressure; packing defects; protein folding and stability; ubiquitin

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Protease de HIV Idioma: En Revista: Proteins Assunto da revista: BIOQUIMICA Ano de publicação: 2015 Tipo de documento: Article

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