Protein stiffening and entropic stabilization in the subdenaturing limit of guanidine hydrochloride.

dc.contributor.author Kumar, Rajesh
dc.contributor.author Prabhu, N. Prakash
dc.contributor.author Yadaiah, M.
dc.contributor.author Bhuyan, Abani K.
dc.date.accessioned 2022-03-27T05:18:56Z
dc.date.available 2022-03-27T05:18:56Z
dc.date.issued 2004-01-01
dc.description.abstract Subdenaturing concentrations of guanidine hydrochloride (GdnHCl) stabilize proteins. For ferrocytochrome c the stabilization is detected at subglobal level with no measured change in global stability. These deductions are made by comparing observed rates of thermally driven ferrocytochrome cHCO reactions with global unfolding rates of ferrocytochrome c measured by stopped flow and NMR hydrogen exchange in the presence of a wide range of GdnHCl concentrations at pH 7, 22 degrees C. Copyright 2004 Biophysical Society
dc.identifier.citation Biophysical journal. v.87(4)
dc.identifier.issn 00063495
dc.identifier.uri 10.1529/biophysj.104.044701
dc.identifier.uri https://www.sciencedirect.com/science/article/abs/pii/S0006349504737364
dc.identifier.uri https://dspace.uohyd.ac.in/handle/1/8022
dc.title Protein stiffening and entropic stabilization in the subdenaturing limit of guanidine hydrochloride.
dc.type Journal. Article
dspace.entity.type
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