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• W2077505087 abstract "We investigated the free energy landscapes of a highly structured beta-hairpin peptide (MBH12) and a less structured peptide with a single mutation of Tyr6 to Asp6 (MBH10). For the free energy mapping, starting from an extended conformation, the replica exchange molecular dynamic simulations for two beta-hairpins were performed using a modified version of an all-atom force field employing an implicit solvation (param99MOD5/GBSA). With the present simulation approach, we demonstrated that detailed stability changes associated with the sequence modification from MBH12 to MBH10 are quantitatively well predicted at the all-atom level." @default.
• W2077505087 created "2016-06-24" @default.
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• W2077505087 date "2008-10-28" @default.
• W2077505087 modified "2023-10-14" @default.
• W2077505087 title "Free energy landscapes of a highly structured β-hairpin peptide and its single mutant" @default.
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• W2077505087 doi "https://doi.org/10.1063/1.3000009" @default.
• W2077505087 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19045319" @default.
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