Complexity in protein folding: Simulation meets experiment
| Title | Complexity in protein folding: Simulation meets experiment |
| Publication Type | Journal Article |
| Year of Publication | 2012 |
| Authors | Caflisch A., Hamm P. |
| Journal | Current Physical Chemistry |
| Volume | 2 |
| Start Page | 4 |
| Issue | 1 |
| Pagination | 4-11 |
| Date Published | Jan 2012 |
| Type of Article | Review Article |
| Keywords | Backbone, Cross-linked alpha-helix, Free energy surface of folding, Kinetic Partitioning, Misfolded traps, molecular dynamics simulations, peptide, Protein Folding, Steric Encumbrance, Time-resolved infrared spectroscopy |
| Abstract | We review our joint experimental-theoretical effort on the folding of photo-switchable α-helices. The folding kinetics of these peptides is profoundly non-exponential, which is attributed to a partitioning of the unfolded state into several misfolded traps. These traps are connected to the folded state in a hub-like fashion with folding barriers of different heights. Molecular dynamics simulations reveal a semi-quantitative agreement with the complex response observed in the experiment, allowing one to discuss the process in unprecedented detail. It is found that the nonexponential response is to a large extent introduced by the photo-linker used to initiate folding. Hence, folding of these cross-linked peptides emulates formation of a helical segment in the context of a globular protein rather than folding of an isolated peptide. |
| DOI | 10.2174/1877946811202010004 |
| pubindex | 0154 |
| Alternate Journal | Curr. Phys. Chem. |
