Document Detail

The diffusion coefficient for PGK folding in eukaryotic cells.
MedLine Citation:
PMID:  21044564     Owner:  NLM     Status:  MEDLINE    
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, the diffusion that controls barrier crossing during protein folding is nearly as fast in cells as in vitro, even though translational diffusion of phosphoglycerate kinase in the cell is slow compared to in vitro.
Apratim Dhar; Simon Ebbinghaus; Zhen Shen; Tripta Mishra; Martin Gruebele
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Publication Detail:
Type:  Comparative Study; In Vitro; Letter; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Biophysical journal     Volume:  99     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-11-03     Completed Date:  2011-01-28     Revised Date:  2013-07-03    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  L69-71     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Department of Chemistry, University of Illinois, Urbana, Illinois, USA.
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MeSH Terms
Biophysical Phenomena
Cell Line
Fluorescence Resonance Energy Transfer
Phosphoglycerate Kinase / chemistry*,  genetics,  metabolism
Protein Folding
Recombinant Fusion Proteins / chemistry,  genetics,  metabolism
Reg. No./Substance:
0/Recombinant Fusion Proteins; EC Kinase

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