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 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.
Kim
Eunae
E
Department of Chemistry, Pusan National University, Busan 609-735, KoreaDepartment of Chemistry, Sejong University, Seoul 143-747, Korea.
Yang
Changwon
C
Jang
Soonmin
S
Pak
Youngshang
Y
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D055550:Protein Stability; D013696:Temperature; D013816:Thermodynamics
D010455:Peptides