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Contributo in rivista
Tipo: Articolo in rivista
Titolo: Molecular modelling of miraculin: Structural analyses and functional hypotheses.
Anno di pubblicazione: 2008
Autori: Paladino A, Costantini S, Colonna G, Facchiano AM.
Abstract: Miraculin is a plant protein that displays the peculiar property of modifying taste by swiching sour into a sweet taste. Its monomer is flavourless at all pH as well as at high concentration; the dimer form elicits its taste-modifying activity at acidic pH; a tetrameric form is also reported as active. Two histidine residues, located in exposed regions, are the main responsible of miraculin activity, as demonstrated by mutagenesis studies. Since structural data of miraculin are not available, we have predicted its three-dimensional structure and simulated both its dimer and tetramer forms by comparative modelling and molecular docking techniques. Finally, molecular dynamics simulations at different pH conditions have indicated that at acidic pH the dimer assumes a widely open conformation, in agreement with the hypotheses coming from other studies.
Pagine da: 26
Pagine a: 32
Biochemical and biophysical research communications
Numero volume: 367
Altre informazioni: 0
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