Folding simulation of Trp-cage utilizing a new AMBER compatible force field with coupled main chain torsions
2014 ◽
Vol 13
(04)
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pp. 1450026
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Keyword(s):
A newly developed AMBER compatible force field with coupled backbone torsion potential terms (AMBER032D) is utilized in a folding simulation of a mini-protein Trp-cage. Through replica exchange and direct molecular dynamics (MD) simulations, a multi-step folding mechanism with a synergetic folding of the hydrophobic core (HPC) and the α-helix in the final stage is suggested. The native structure has the lowest free energy and the melting temperature predicted from the specific heat capacity Cvis only 12 K higher than the experimental measurement. This study, together with our previous study, shows that AMBER032Dis an accurate force field that can be used for protein folding simulations.
2015 ◽
Vol 112
(38)
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pp. 11846-11851
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2017 ◽
Keyword(s):
2020 ◽
Keyword(s):
2020 ◽
Keyword(s):
2015 ◽
Vol 11
(11)
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pp. 5473-5480
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1985 ◽
Vol 63
(11)
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pp. 1167-1175
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2016 ◽
Vol 374
(2060)
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pp. 20150032
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