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Guanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species.

The kinetics of the refolding reaction of ribonuclease A from high concentrations of guanidine hydrochloride or urea are biphasic, and show two refolding reactions whose rates differ 450-fold at pH 5.8 and 25 degrees. Measurements of cytidine 2'-phosphate binding during refolding, after stopped...

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Detalles Bibliográficos
Main Authors: Garel, J R, Nall, B T, Baldwin, R L
Formato: Artigo
Idioma:Inglês
Publicado: 1976
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC430405/
https://ncbi.nlm.nih.gov/pubmed/1064858
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