Residue-level interrogation of macromolecular crowding effects on protein stability.
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ABSTRACT:
SUBMITTER: Charlton LM
PROVIDER: S-EPMC2435214 | biostudies-literature | 2008 May
REPOSITORIES: biostudies-literature
Publications
Residue-level interrogation of macromolecular crowding effects on protein stability.
Charlton Lisa M LM Barnes Christopher O CO Li Conggang C Orans Jillian J Young Gregory B GB Pielak Gary J GJ
Journal of the American Chemical Society 20080507 21
Theory predicts that macromolecular crowding affects protein behavior, but experimental confirmation is scant. Herein, we report the first residue-level interrogation of the effects of macromolecular crowding on protein stability. We observe up to a 100-fold increase in the stability, as measured by the equilibrium constant for folding, for the globular protein chymotrypsin inhibitor 2 (CI2) in concentrations of the cosolute poly(vinylpyrrolidone) (PVP) that mimic the protein concentration in ce ...[more]
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