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

SummaryA 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.

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