Journal article icon

Journal article

A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein.

Abstract:

Insights into the conformational passage of a polypeptide chain across its free energy landscape have come from the judicious combination of experimental studies and computer simulations. Even though some unfolded and partially folded proteins are now known to possess biological function or to be involved in aggregation phenomena associated with disease states, experimentally derived atomic-level information on these structures remains sparse as a result of conformational heterogeneity and dy...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1038/nature05728

Authors


Journal:
Nature More from this journal
Volume:
447
Issue:
7140
Pages:
106-109
Publication date:
2007-05-01
DOI:
EISSN:
1476-4687
ISSN:
0028-0836
Language:
English
Keywords:
Pubs id:
pubs:33816
UUID:
uuid:cb5e7855-7cc7-4f1d-b9de-a822b0621baa
Local pid:
pubs:33816
Source identifiers:
33816
Deposit date:
2012-12-19

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP