Multi-conformational peptide dynamics derived from NMR data: A new search algorithm and its application to antamanide

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Abstract
A search algorithm, called MEDUSA, is presented which allows the determination of multiple conformations of biomolecules in solution with exchange rate constants typically between 103 and 107 s−1 on the basis of experimental high-resolution NMR data. Multiples of structures are generated which are consistent as ensembles with NMR cross-relaxation rates (NOESY, ROESY), scalar J-coupling constants, and T1p measurements. The algorithm is applied to the cyclic decapeptide antamanide dissolved in chloroform. The characteristic radio-frequency field dependence of the T1p relaxation rates found for the NH protons of Val1 and Phe6 can be explained by a dynamical exchange between two structures.