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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 …