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Title: | Crystal structure of the sweet-tasting protein thaumatin II at 1.27Å. |
Authors: | Masuda, Tetsuya ![]() ![]() ![]() Ohta, Keisuke Tani, Fumito ![]() ![]() Mikami, Bunzo ![]() ![]() Kitabatake, Naofumi |
Author's alias: | 桝田, 哲哉 |
Keywords: | Thaumatin Sweet-tasting protein Amino-acid variations Positive charge |
Issue Date: | 8-Jul-2011 |
Publisher: | Elsevier Inc. |
Journal title: | Biochemical and biophysical research communications |
Volume: | 410 |
Issue: | 3 |
Start page: | 457 |
End page: | 460 |
Abstract: | 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 Å. Overall structure of thaumatin II is similar to thaumatin I, but a slight shift of the Cα 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. |
Rights: | © 2011 Elsevier Inc. This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 |
URI: | http://hdl.handle.net/2433/175268 |
DOI(Published Version): | 10.1016/j.bbrc.2011.05.158 |
PubMed ID: | 21672520 |
Appears in Collections: | Journal Articles |

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