학술논문
Micelle-bound conformations of a bombesin/gastrin releasing peptide receptor agonist and an antagonist by two-dimensional NMR and restrained molecular dynamics
Document Type
Academic Journal
Source
Biochemistry. August 11, 1992, Vol. 31 Issue 31, p7043, 7 p.
Subject
Language
ISSN
0006-2960
Abstract
The conformations of two micelle-bound nonapeptide analogs of the carboxyl ends of gastrin-releasing peptide and bombesin were determined using restrained molecular dynamics simulation utilizing interproton distances computed from two-dimensional nuclear magnetic resonance as constraints. One of the analogs is an agonist of the hormone receptor while the other is an antagonist. Results indicate that both analogs have a relaxed helical conformation. Two turns in the amino terminal are similar for both peptides but the third turn in the carboxyl terminus of the agonist is absent in the antagonist.