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Matching Simulation and Experiment: a New Simpliied Model for Simulating Protein Folding (extended Abstract) a Simpliied Model for Protein Folding
| Content Provider | Semantic Scholar |
|---|---|
| Author | Sorenson, Jon M. Head-Gordon, Teresa |
| Copyright Year | 1999 |
| Abstract | Simulations of simpliied protein folding models have provided much insight into solving the protein folding problem. We propose here a new oo-lattice bead model, capable of simulating several diierent fold classes of small proteins. We present the sequence for an == protein resembling the IgG-binding proteins L and G. The thermodynamics of the folding process for this model are characterized using the multiple multi-histogram method combined with constant-temperature Langevin simulations. The folding is shown to be highly cooperative, with chain collapse nearly accompanying folding. Two parallel folding pathways are shown to exist on the folding free energy landscape. One pathway contains an intermediate|similar to experiments on protein G, and one pathway contains no intermediates|similar to experiments on protein L. The folding kinetics are characterized by tabulating mean-rst passage times, and we show that the onset of glasslike kinetics occurs at much lower temperatures than the folding temperature. This model is expected to be useful in many future contexts: investigating questions of the role of local versus non-local interactions in various fold classes, addressing the eeect of sequence mutations aaecting secondary structure propensities, and providing a computationally feasible model for studying the role of solvation forces in protein folding. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://polygon.lbl.gov/jsorenso/mixed/mixed.ps.gz |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
