期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 108, 期 31, 页码 12734-12739出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1010880108
关键词
protein dynamics; near-native dynamics
资金
- National Science Foundation [CNS-0619926, EF-0623664, MCB-0954714, DMS-0900700]
- Burroughs-Wellcome Career Award
- Stanford Graduate Fellowship
- National Institutes of Health [R01-GM062868, U54-GM072970]
As the fastest folding protein, the villin headpiece (HP35) serves as an important bridge between simulation and experimental studies of protein folding. Despite the simplicity of this system, experiments continue to reveal a number of surprises, including structure in the unfolded state and complex equilibrium dynamics near the native state. Using 2.5 ms of molecular dynamics and Markov state models, we connect to current experimental results in three ways. First, we present and validate a novel method for the quantitative prediction of triplet-triplet energy transfer experiments. Second, we construct a many-state model for HP35 that is consistent with previous experiments. Finally, we predict contact-formation time traces for all 1,225 possible triplet-triplet energy transfer experiments on HP35.
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