ISSN:
1075-2617
Keywords:
peptide T
;
AMBER force field
;
conformation
;
bioactive peptide
;
molecular mechanics
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The conformational preferences of peptide T (ASTTTNYT) were analysed by means of computational methods. A thorough exploration of the conformational space was carried out within the framework of the molecular mechanics approach, using simulated annealing as a searching strategy. Specifically, in order to obtain a subset of low-energy conformations with energies close to the global minimum as complete as possible, a simulated annealing protocol was repeated several times in a recursive fashion. The results of the search indicate that the peptide exhibits a α-helical character although most of the conformations characterized, including the global minimum, can be described as bent conformations. Conformations exhibiting β-turn motives previously proposed from NMR studies were also characterized, although they are not very predominant in the set of low-energy conformations. © 1997 European Peptide Society and John Wiley & Sons, Ltd.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
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