CONFORMATIONAL STUDY OF VALINOMYCIN - A MOLECULAR-DYNAMICS APPROACH

Valinomycin is a highly flexible cyclic dodecadepsipeptide that transp orts ions across membranes. Such a flexibility in the conformation is required for its biological function since it has to encounter a varie ty of environments and liganding state. Exploration of conformational space of this molecule is therefore important and is one of the object ives of the present study that has been carried out by means of high t emperature Molecular Dynamics. Further, the stability of the known bra celet-like structure of the uncomplexed valinomycin and the inherent f lexibility around this structure has been investigated. The uncomplexe d form of valinomycin has been simulated at 75-100 K for 1 ns in order to elucidate the average conformational properties. An alanine-analog of valinomycin has been simulated under identical conditions in order to evaluate the effect of sidechain on the conformational properties, The studies confirm the effect of sidechain on conformational equilib rium.