Initial hydrophobic collapse is not necessary for folding RNase A

Item Type:	Article
Title:	Initial hydrophobic collapse is not necessary for folding RNase A
Creators Name:	Noeppert, A. and Gast, K. and Zirwer, D. and Damaschun, G.
Abstract:	BACKGROUND: One of the main distinctions between different theories describing protein folding is the predicted sequence of secondary structure formation and compaction during the folding process. Whether secondary structure formation precedes compaction of the protein molecules or secondary structure formation is driven by a hydrophobic collapse cannot be decided unequivocally on the basis of existing experimental data. RESULTS: In this study, we investigate the refolding of chemically denatured, disulfide-intact ribonuclease A (RNase A) by monitoring compaction and secondary structure formation using stopped-flow dynamic light scattering and stopped-flow CD, respectively. Our data reveal the formation of a considerable amount of secondary structure early in the refolding of the slow folding species of RNase A without a significant compaction of the molecules. A simultaneous formation of secondary structure and compaction is observed in the subsequent rate-limiting step of folding. CONCLUSIONS: During folding of RNase A an initial global hydrophobicity is not observed, which contradicts the view that this is a general requirement for protein folding. This folding behavior could be typical of similar, moderately hydrophobic proteins.
Keywords:	Folding Model, Protein Folding, RNase A, Stopped-Flow CD, Stopped-Flow DLS
Source:	Folding & Design
ISSN:	1359-0278
Publisher:	Current Biology
Volume:	3
Number:	3
Page Range:	213-221
Date:	June 1998
Official Publication:	https://doi.org/10.1016/S1359-0278(98)00029-7
PubMed:	View item in PubMed

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