Ontology highlight
ABSTRACT:
SUBMITTER: Cho SS
PROVIDER: S-EPMC2224170 | biostudies-literature | 2008 Jan
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20080102 1
In contrast to classical chemical phenomenology, theory suggests that proteins may undergo downhill folding without an activation barrier under certain thermodynamic conditions. Recently, the BBL protein was proposed to fold by such a downhill scenario, but discrepancies between experimental results found in different groups argue against this. After briefly reviewing the major experimental studies of the BBL folding mechanism, we show that simulations of both coarse-grained and atomistic models ...[more]