Protein Folding Under an Applied Force
Public DepositedIn this thesis we study protein folding with external force. In Part I we simulate the folding or unfolding procedure based on the two-state model. For constant-velocity experiments, the simulation results fit the experimental results. For constant-force experiments, we introduce cooperativity between domains to explain the different behavior between single domain folding and multi-domain folding. To make the simulation results fit the experimental results, in Part I we have to set the folding rates to unreasonable values. In Part II we solve this problem. In this part we present a model in which folding is comprised of smaller motions individually acted upon by the applied force. The model naturally explains how cooperativity arises when an applied force is present and why observed folding times become less sensitive to the external force as force increases, while the two-state model predicts the opposite trend.
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umi-northwestern-2029.pdf | 2018-09-14 | Public |
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