期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 410, 期 3, 页码 457-460出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2011.05.158
关键词
Thaumatin; Sweet-tasting protein; Amino-acid variations; Positive charge
资金
- Japan Society for the Promotion of Science [19780074, 22580105]
- Japan Food Chemical Research Foundation
- Grants-in-Aid for Scientific Research [19780074, 22580105] Funding Source: KAKEN
Thaumatin, an intensely sweet-tasting protein, elicits a sweet taste sensation at 50 nM. Here the X-ray crystallographic structure of one of its variants, thaumatin II, was determined at a resolution of 1.27 angstrom. Overall structure of thaumatin II is similar to thaumatin I, but a slight shift of the C alpha atom of G96 in thaumatin II was observed. Furthermore, the side chain of residue 67 in thaumatin II is highly disordered. Since residue 67 is one of two residues critical to the sweetness of thaumatin, the present results suggested that the critical positive charges at positions 67 and 82 are disordered and the flexibility and fluctuation of these side chains would be suitable for interaction of thaumatin molecules with sweet receptors. (C) 2011 Elsevier Inc. All rights reserved.
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