Computational Study of Human Calcitonin (hCT) Oligomer

We have performed long time REMD simulation on 15-19 residues of human calcitonin hormone (DFNKF) which is known to form highly ordered amyloid fibril. The simulation started from randomly oriented multiple DFNKF strand. Using all-atom level simulations with the generalized Born solvation (GB) model...

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Bibliographic Details
Published inBulletin of the Korean Chemical Society Vol. 30; no. 12; pp. 3006 - 3010
Main Authors Pak, Young-Shang, Shin, Jung-Ho, Jang, Soon-Min
Format Journal Article
LanguageKorean
Published 2009
Subjects
Computational chemistry
Human calcitonin (hCT)
Amyloid
Molecular dynamics simulation
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Summary:We have performed long time REMD simulation on 15-19 residues of human calcitonin hormone (DFNKF) which is known to form highly ordered amyloid fibril. The simulation started from randomly oriented multiple DFNKF strand. Using all-atom level simulations with the generalized Born solvation (GB) model (param99MOD3), we observed spontaneous formation of ${\beta}$-sheet for tetramer. Interestingly, the current simulation gives anti-parallel sheet as a major conformation, consistent with experiments. The major interaction stabilizing the anti-parallel sheet seems to be the inter-strand hydrogen bond.
Bibliography:KISTI1.1003/JNL.JAKO200902727152847
ISSN:0253-2964
1229-5949