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Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.
Charlier, Cyril; Alderson, T Reid; Courtney, Joseph M; Ying, Jinfa; Anfinrud, Philip; Bax, Adriaan.
  • Charlier C; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
  • Alderson TR; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
  • Courtney JM; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
  • Ying J; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
  • Anfinrud P; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520 philip.anfinrud@nih.gov bax@nih.gov.
  • Bax A; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520 philip.anfinrud@nih.gov bax@nih.gov.
Proc Natl Acad Sci U S A ; 115(18): E4169-E4178, 2018 05 01.
Article en En | MEDLINE | ID: mdl-29666248
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Pliegue de Proteína / Resonancia Magnética Nuclear Biomolecular / Ubiquitina Límite: Humans Idioma: En Año: 2018 Tipo del documento: Article
Texto completo
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PubMed Links
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Pliegue de Proteína / Resonancia Magnética Nuclear Biomolecular / Ubiquitina Límite: Humans Idioma: En Año: 2018 Tipo del documento: Article