Toward the understanding of MNEI sweetness from hydration map surfaces.

ABSTRACT: The binding mechanism of sweet proteins to their receptor, a G-protein-coupled receptor, is not supported by direct structural information. In principle, the key groups responsible for biological activity (glucophores) can be localized on a small structural unit (sweet finger) or spread on a larger surface area. A recently proposed model, called "wedge model", implies a large surface of interaction with the receptor. To explore this model in greater detail, it is necessary to examine the physicochemical features of the surfaces of sweet proteins, since their interaction with the receptor, with respect to that of small sweeteners, is more dependent on general physicochemical properties of the interface, such as electrostatic potential and hydration. In this study, we performed exhaustive mo

SUBMITTER: De Simone A 

PROVIDER: S-EPMC1432101 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature