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Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.

We have measured the rate constants for exchange of amide protons in 15N-labeled wild-type barnase and a disulfide mutant that is more stable by 2 kcal.mol-1. The relative rate constants for exchange for wild type and mutant should reflect the changes in the equilibrium constants for local or global...

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Detalles Bibliográficos
Publicado en:Proc Natl Acad Sci U S A
Principais autores: Clarke, J, Hounslow, A M, Bycroft, M, Fersht, A R
Formato: Artigo
Idioma:Inglês
Publicado: National Academy of Sciences 1993
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Acceso en liña:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC47667/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8234322/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.90.21.9837
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