STUDYING THE STABILITY OF A HELICAL BETA-HEPTAPEPTIDE BY MOLECULAR-DYNAMICS SIMULATIONS

Citation
X. Daura et al., STUDYING THE STABILITY OF A HELICAL BETA-HEPTAPEPTIDE BY MOLECULAR-DYNAMICS SIMULATIONS, Chemistry, 3(9), 1997, pp. 1410-1417
Citations number
19
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry
Journal title
Chemistry → ACNP
ISSN journal
0947-6539
Volume
3
Issue
9
Year of publication
1997
Pages
1410 - 1417
Database
ISI
SICI code
0947-6539(1997)3:9<1410:STSOAH>2.0.ZU;2-W
Abstract
beta-Peptides consisting entirely of homochiral beta-amino acids R-CH( NH2)-CH2CO2H form 3(1)-helices in solution, as shown previously by NMR analysis of pyridine and methanol solutions. The stability of the hel ical secondary structure of one such beta-peptide eta-HVal-beta-HAla-b eta-HLeu-(S,S)-beta-HAla(alpha Me)-beta-HVal-beta- HAla-beta-HLeu-OH, 1) has been investigated by molecular dynamics simulations using the G ROMOS96 molecular model and force field (962 methanol molecules: T = 2 98, 350, 400 K; with and without NOE distance restraints). The restrai nts derived from the NMR studies were equally well satisfied by both t he restrained and the unrestrained room-temperature molecular dynamics simulations. The 3(1)-helical conformation of 1 was shown to be so st able that it was restored spontaneously within 400 ps after unfolding had been induced by a sudden increase of the temperature from 298 to 3 50 K.