Kinetics are probe-dependent during downhill folding of an engineered lambda6-85 protein.
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ABSTRACT:
SUBMITTER: Ma H
PROVIDER: S-EPMC548978 | biostudies-literature | 2005 Feb
REPOSITORIES: biostudies-literature
Publications
Kinetics are probe-dependent during downhill folding of an engineered lambda6-85 protein.
Ma Hairong H Gruebele Martin M
Proceedings of the National Academy of Sciences of the United States of America 20050207 7
The Y22W/Q33Y/G46,48A mutant of the protein lambda6-85 folds in a few microseconds at room temperature. We find that its folding kinetics are probe-dependent under a strong bias toward the native state, a new signature for downhill folding. The IR- and fluorescence-detected relaxation time scales converge when the native bias is removed by raising the temperature, recovering activated two-state folding. Langevin dynamics simulations on one- and 2D free energy surfaces tunable from two-state to d ...[more]
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