Minimal model for studying prion-like folding pathways |
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Authors: | Chen Jeff Z Y Lemak Alexander S Lepock James R Kemp Josh P |
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Affiliation: | Department of Physics, University of Waterloo, Waterloo, Ontario, Canada. jeffchen@onsager.uwaterloo.ca |
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Abstract: | The Monte Carlo technique is used to simulate the energy landscape and the folding kinetics of a minimal prion-like protein model. We show that the competition between hydrogen-bonding and hydrophobic interactions yields two energetically favored secondary structures, an alpha-helix and a beta-hairpin. Folding simulations indicate that the probability of reaching the alpha-helix form from a denatured random conformation is much higher than the probability of reaching the beta-sheet form, even though the beta-sheet has a lower energy. The existence of a lower energy beta-sheet state gives the possibility for the normal alpha-helix structure to take a structural transformation into the beta-sheet structure under external influences. |
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Keywords: | minimal model proteins prion folding pathway Monte Carlo simulation |
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