Molecular mechanisms of sweet taste 7: The sweet protein, Thaumatin I

被引：3
|
作者：
Suami, T
Hough, L
Machinami, T
Watanabe, N
Nakamura, R
机构：
[1] UNIV LONDON KINGS COLL, DEPT CHEM, LONDON W8 7AH, ENGLAND
[2] IWAKI MEISEI UNIV, COLL SCI & ENGN, DEPT CHEM, HINO, TOKYO 191, JAPAN
[3] AJINOMOTO CO INC, DEPT SYST ENGN, KAWASAKI, KANAGAWA 210, JAPAN
来源：
FOOD CHEMISTRY | 1997年 / 60卷 / 03期
关键词：
D O I：
10.1016/S0308-8146(96)00284-1
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
A computer modelling study of the host-guest relationship between the intensely sweet protein named Thaumatin I and our suggested receptor model, an alpha-helical protein, has revealed a perfect fit within a cleft of the Thaumatin I conformation. The parameters and stereoselective interactions for the initiation of the sweetness sensation are interpreted in accord with our previous stereo-interactive studies on a wide range of low molecular weight sweeteners. Also, the Thaumatin data parallels that of the macromolecular sweet protein Monellin, and their intense sweetness arises from the multiple interactions arising within the docking cleft of the protein receptor. The AH(s)/B-s pair of Thaumatin I has been assigned to Lys-97/Asp-98. (C) 1997 Elsevier Science Ltd.
引用
收藏
页码：277 / 285
页数：9
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