Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell
UNSPECIFIED (2000) Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. In: EMBO Workshop on Functional Organization of the Cell Nucleus, AUG 09-12, 1999, PRAGUE, CZECH REPUBLIC.Full text not available from this repository.
We have studied the effects of macromolecular crowding on protein folding kinetics by studying the oxidative refolding of hen lysozyme in the absence and presence of high concentrations of bovine serum albumin and Ficoll 70, The heterogeneity characteristic of the lysozyme refolding process is preserved under crowded conditions. This, together with the observation that the refolding intermediates that accumulate to significant levels are very similar in the absence and presence of Ficoll, suggests that crowding does not alter substantially the energetics of the protein folding reaction. However, the presence of high concentrations of macromolecules results in the acceleration of the fast track of the refolding process whereas the slow track is substantially retarded, The results can be explained by preferential excluded volume stabilization of compact states relative to more unfolded states, and suggest that, relative to dilute solutions, the rates of many protein folding processes are likely to be altered under conditions that more closely resemble the intracellular environment.
|Item Type:||Conference Item (UNSPECIFIED)|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||EMBO JOURNAL|
|Publisher:||OXFORD UNIV PRESS|
|Date:||1 August 2000|
|Number of Pages:||6|
|Page Range:||pp. 3870-3875|
|Title of Event:||EMBO Workshop on Functional Organization of the Cell Nucleus|
|Location of Event:||PRAGUE, CZECH REPUBLIC|
|Date(s) of Event:||AUG 09-12, 1999|
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