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Modulating Native-like Residual Structure in the Fully Denatured State of Photoactive Yellow Protein Affects Its Refolding

Residual structure in the fully unfolded state is a key element for understanding protein folding. We show that the residual structure in fully denatured photoactive yellow protein (PYP) is affected by isomerization of its p-coumaric acid (pCA) chromophore. The exposure of total surface area and hyd...

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Detalhes bibliográficos
Main Authors: Lee, Byoung-Chul, Kumauchi, Masato, Hoff, Wouter D.
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2010
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2857096/
https://ncbi.nlm.nih.gov/pubmed/20178976
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.065821
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