volume 82, issue 11, P2970-2981 2014
DOI: 10.1002/prot.24654
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Abstract: An AK16 peptide and a C-peptide analog are experimentally known to form more helical structures under high-pressure conditions than those at atmospheric pressure, even though most proteins usually unfold at high pressure. To understand the pressure-induced structural changes of the two peptides, molecular dynamics simulations with the simulated tempering method for the isobaric-isothermal ensemble were performed in a wide pressure range from 0.1 MPa to 1.4 GPa. We found that the fraction of the folded state de…

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