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:12149462Additional Information
Study Summary
| Number of data points | 2 |
| Proteins | 30S ribosomal protein S6 ; 30S ribosomal protein S6 |
| Unique complexes | 1 |
| Assays/Quantities/Protocols | Experimental Assay: m ; Experimental Assay: dG_H2O |
| Libraries | Mutations for sequence MRRYEVNIVLNPNLDQSQLALEKEIIQRALENYGARVEKVEELGLRRLAYPIAKDPQGYFLWYQVEMPEDRVNDLARELRIRDNVRRVMVVKSQEPFLANA |
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Data Distribution
Studies with similar sequences (approximate matches)