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Molecular dynamics study of major urinary protein-pheromone interactions: a structural model for ligand-induced flexibility increase
Macek P, Novák P, Krízová H, Zídek L, Sklenár V.
Jazyk angličtina Země Nizozemsko
NLK
Free Medical Journals
od 1968 do 2015
ScienceDirect (archiv)
od 1993-01-01 do 2009-12-31
Wiley Free Content
od 1997 do Před 1 rokem
- MeSH
- feromony chemie metabolismus MeSH
- financování organizované MeSH
- molekulární modely MeSH
- počítačová simulace MeSH
- protein - isoformy chemie metabolismus MeSH
- proteiny chemie metabolismus MeSH
- terciární struktura proteinů MeSH
- vodíková vazba MeSH
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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- $a 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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