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Folded conformation of an immunostimulating tetrapeptide rigin: high temperature molecular dynamics simulation study.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Folded conformation of an immunostimulating tetrapeptide rigin: high temperature molecular dynamics simulation study.
 
Creator Ashish, A
Kishore, Raghuvansh
 
Subject QD Chemistry
 
Description Employing high temperature quenched molecular dynamics (QMD) stimulations the conformational energy space of an immunostimulating tetrapeptide rigin: H-Gly341-Gln-Pro-Arg344-OH, is explored. Using distance dependent dielectric (epsilon =r(ij)) 31 different low energy starting structures with identical sequence were computed for their conformational preferences. According to the hypothesis of O'Connors et al. [J. Med. Chem. 35 (1992), 2870], 83 low-energy conformers resulted from unrestrained molecular dynamics (MD) simulations, could be classified into two energy minimized families: A and B, comprised of 64 (Pro C(gamma)-endo orientation) and 19 (Pro C(gamma)-exo orientation) structures, respectively. An examination of these families revealed the existence of a remarkably similar folded backbone conformation: torsion angles being phi(i+1) approximately -65 degrees, psi(i+1) approximately -65 degrees, phi(i+2) approximately -65 degrees, psi(i+2) approximately -60 degrees, characterizing a distorted type III beta-turn structure across the central Gln-Pro segment. The folded conformation of rigin is devoid of a classical 1
 
Publisher Elsevier Science
 
Date 2002-12
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/260/1/kishore2002.pdf
Ashish, A and Kishore, Raghuvansh (2002) Folded conformation of an immunostimulating tetrapeptide rigin: high temperature molecular dynamics simulation study. Bioorganic & medicinal chemistry, 10 (12). pp. 4083-90. ISSN 0968-0896
 
Relation http://www.sciencedirect.com/science/article/pii/S0968089602003012
http://crdd.osdd.net/open/260/