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Computational Study of the Conformational Domains of Peptide T

✍ Scribed by Marta Filizola; Nuria B. Centeno; Juan J. Perez

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 243 KB
Volume: 3
Category: Article
ISSN: 1075-2617
DOI: 10.1002/(sici)1099-1387(199703)3:2<85::aid-psc84>3.0.co;2-0

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✦ Synopsis

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 a-helical character although most of the conformations characterized, including the global minimum, can be described as bent conformations. Conformations exhibiting b-turn motives previously proposed from NMR studies were also characterized, although they are not very predominant in the set of low-energy conformations.

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