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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Pande, Vijay S. Ensign, Daniel L. Das, Rhiju Beauchamp, Kyle A. |
| Description | Author Affiliation: Beauchamp KA ( Biochemistry, Physics, and Chemistry Departments, Stanford University, Stanford, CA 94305, USA.); |
| Abstract | 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 31 |
| Volume Number | 108 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2011-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Energy Transfer Microfilament Proteins Chemistry Molecular Dynamics Simulation Protein Structure, Tertiary Electron Transport Kinetics Genetics Metabolism Models, Chemical Models, Molecular Mutation Protein Conformation Protein Folding Protein Structure, Secondary Comparative Study Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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