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Restrained and unrestrained molecular dynamics simulations in the NVT ensemble of alamethicin
Author(s) -
Fraternali F.
Publication year - 1990
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360301109
Subject(s) - alamethicin , molecular dynamics , chemistry , molecule , chemical physics , crystallography , computational chemistry , membrane , lipid bilayer , biochemistry , organic chemistry
Molecular dynamics simulations on the transmembrane antibiotic peptide alamethicin have been performed in the NVT ensamble (i.e., the number of particles N , the volume V , and the temperature T of the system are kept constant). Results on the structure and conformational flexibility of this molecule are discussed and compared with previous experimental CD, x‐ray, nmr data and theoretical computations on fragments analogues. An extensive study of structural and dynamic properties from H‐bonding pattern analysis is presented. Evidences for a largely α‐helix structure with some extent of freedom in the C‐terminal region are found. Further, a partition of the molecule into three regions on the base of structural features and dynamic behavior has been proposed, and the correlation among the motions of the three regions is described.