Experimental evaluation of topological parameters determining protein-folding rates.
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.
Miller
Erik J
EJ
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Fischer
Kael F
KF
Marqusee
Susan
S
D007700:Kinetics; D017510:Protein Folding; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics; D016963:Thermus thermophilus / Q000737:chemistry* / Q000235:genetics
D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins