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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.

SUBMITTER: Miller EJ 

PROVIDER: S-EPMC124919 | biostudies-literature | 2002 Aug

REPOSITORIES: biostudies-literature

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Experimental evaluation of topological parameters determining protein-folding rates.

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]

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