Free energy landscapes of a highly structured beta-hairpin peptide and its single mutant

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...

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Bibliographic Details
Published inThe Journal of chemical physics Vol. 129; no. 16; p. 165104
Main Authors Kim, Eunae, Yang, Changwon, Jang, Soonmin, Pak, Youngshang
Format Journal Article
LanguageEnglish
Published United States 28.10.2008
Subjects
Amino Acid Sequence
Models, Molecular
Molecular Sequence Data
Mutation
Peptides - chemistry
Peptides - genetics
Peptides - metabolism
Protein Conformation
Protein Folding
Protein Stability
Temperature
Thermodynamics
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Summary: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.
ISSN:1089-7690
DOI:10.1063/1.3000009