Unknown

Dataset Information

0

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

altmetric image

Publications

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]

Similar Datasets

2013-11-25 | GSE51915 | GEO
2013-11-25 | E-GEOD-51915 | biostudies-arrayexpress
| S-EPMC6510998 | biostudies-literature
2020-06-24 | GSE136056 | GEO
2024-03-26 | PXD045601 | Pride
| S-EPMC7427326 | biostudies-literature
| S-EPMC2963614 | biostudies-literature
2011-12-01 | E-GEOD-27062 | biostudies-arrayexpress
| S-EPMC3376171 | biostudies-literature
| S-EPMC4380988 | biostudies-literature