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The B domain of protein A retains residual structures in 6 M guanidinium chloride as revealed by hydrogen/deuterium‐exchange NMR spectroscopy

The characterization of residual structures persistent in unfolded proteins is an important issue in studies of protein folding, because the residual structures present, if any, may form a folding initiation site and guide the subsequent folding reactions. Here, we studied the residual structures of...

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Detalles Bibliográficos
Autores principales: Yanaka, Saeko, Yagi‐Utsumi, Maho, Kato, Koichi, Kuwajima, Kunihiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9926473/
https://www.ncbi.nlm.nih.gov/pubmed/36659853
http://dx.doi.org/10.1002/pro.4569