Experimental evaluation of topological parameters determining protein-folding rates.


Abstract

Recent work suggests that structural topology plays a key role in determining protein-folding rates and pathways. The refolding rates of small proteins that fold without intermediates are found to correlate with simple structural parameters such as relative contact order, long-range order, or the fraction of short-range contacts. To test and evaluate the role of structural topology experimentally, a set of circular permutants of the ribosomal protein S6 from Thermus thermophilus was analyzed. Despite a wide range of relative contact order, the permuted proteins all fold with similar rates. These results suggest that alternative topological parameters may better describe the role of topology in protein-folding rates. Study holds ProTherm entries: 15452 Extra Details: structural topology; contact order; long-range order; protein-folding rates

Submission Details

ID: WvW6DfPE4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:46 p.m.

Version: 1

Publication Details
Miller EJ;Fischer KF;Marqusee S,Proc. Natl. Acad. Sci. U.S.A. (2002) Experimental evaluation of topological parameters determining protein-folding rates. PMID:12149462
Additional Information

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