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
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:46 p.m.
|Number of data points||2|
|Proteins||30S ribosomal protein S6 ; 30S ribosomal protein S6|
|Assays/Quantities/Protocols||Experimental Assay: m ; Experimental Assay: dG_H2O|
|Libraries||Mutations for sequence MRRYEVNIVLNPNLDQSQLALEKEIIQRALENYGARVEKVEELGLRRLAYPIAKDPQGYFLWYQVEMPEDRVNDLARELRIRDNVRRVMVVKSQEPFLANA|