Ontology highlight
ABSTRACT:
SUBMITTER: Miller EJ
PROVIDER: S-EPMC124919 | biostudies-literature | 2002 Aug
REPOSITORIES: biostudies-literature
Miller Erik J EJ Fischer Kael F KF Marqusee Susan S
Proceedings of the National Academy of Sciences of the United States of America 20020729 16
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. De ...[more]