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ABSTRACT:
SUBMITTER: Dhar A
PROVIDER: S-EPMC2965994 | biostudies-literature | 2010 Nov
REPOSITORIES: biostudies-literature
Dhar Apratim A Ebbinghaus Simon S Shen Zhen Z Mishra Tripta T Gruebele Martin M
Biophysical journal 20101101 9
We compare the folding kinetics of a fluorescent phosphoglycerate kinase construct in 30 mammalian cells with that in aqueous buffer. In both environments, the kinetics can be fitted to the functional form exp[-(t/τ)(β)]. A histogram of τ shows that the average folding relaxation time in cells is only twice as long as in aqueous buffer. Consideration of the folding free energy and of β reveals that only some of the variation in τ arises from perturbation of the protein's energy landscape. Thus, ...[more]