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  • Title: Molecular dynamics study of major urinary protein-pheromone interactions: a structural model for ligand-induced flexibility increase.
    Author: Macek P, Novák P, Krízová H, Zídek L, Sklenár V.
    Journal: FEBS Lett; 2006 Jan 23; 580(2):682-4. PubMed ID: 16412435.
    Abstract:
    Recently, two independent (15)N NMR relaxation studies indicated that in contrast to the decreased flexibility expected for induced-fit interactions, the backbone flexibility of major urinary protein isoform I (MUP-I) slightly increased upon complex formation with its natural pheromone 2-sec-butyl-4,5-dihydrothiazol. We have investigated the subtle details of molecular interactions by molecular dynamics simulations in explicit solvent. The calculated order parameters S(2) for a free- and ligand-bound protein supply evidence that mobility in various regions of MUP-I can be directly related to small conformational changes of the free- and complexed protein resulting from modifications of the hydrogen bonding network.
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