ISSN:
0947-6539
Keywords:
helical structures
;
molecular dynamics simulations
;
NMR spectroscopy
;
peptides
;
Chemistry
;
General Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
β-Peptides consisting entirely of homochiral β-amino acids R-CH(NH2)-CH2CO2H form 31-helices in solution, as shown previously by NMR analysis of pyridine and methanol solutions. The stability of the helical secondary structure of one such β-peptide (H-β-HVal-β-HAla-β-HLeu-(S,S)-β-HAla(αMe)-β-HVal-β-HAla-β-HLeu-OH, 1) has been investigated by molecular dynamics simulations using the GROMOS 96 molecular model and force field (962 methanol molecules; T = 298, 350, 400 K; with and without NOE distance restraints). The restraints derived from the NMR studies were equally well satisfied by both the restrained and the unrestrained room-temperature molecular dynamics simulations. The 31-helical conformation of 1 was shown to be so stable that it was restored spontaneously within 400 ps after unfolding had been induced by a sudden increase of the temperature from 298 to 350 K.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/chem.19970030907
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