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Structure and Dynamics of Angiotensin (1‐7) Vasoactive Peptide in Aqueous Solution at the Density‐Functional Based Tight‐Binding Level
Author(s) -
de Lima Guilherme Ferreira,
Heine Thomas,
Duarte Hélio A.
Publication year - 2007
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.200750812
Subject(s) - aqueous solution , solvation , molecular dynamics , chemistry , solvation shell , molecule , computational chemistry , intermolecular force , solvent , peptide , density functional theory , hydrogen bond , chemical physics , organic chemistry , biochemistry
Summary : Structure and dynamics of heptapeptide Angiotensin (1‐7) in aqueous solution have been investigated by means of density‐functional based tight‐binding molecular dynamics simulations. Solvent‐solute interactions have been studied using a hybrid QM/MM method. The backbone of the heptapeptide remains relatively rigid in aqueous solution compared to gas phase. The solvent acts as a cushion, preventing the free motion of the molecule. Tyrosine is the residue which presents the smallest flexibility and the largest number of water molecules in its first solvation shell. This is in good agreement with the previously published NMR results. The intra– and intermolecular hydrogen bridges have been quantified and analyzed in terms of conformation and stability.