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Title: Crystal structure of the sweet-tasting protein thaumatin II at 1.27Å.
Authors: Masuda, Tetsuya  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-5857-5753 (unconfirmed)
Ohta, Keisuke
Tani, Fumito  kyouindb  KAKEN_id
Mikami, Bunzo  kyouindb  KAKEN_id
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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