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エンドウ トシヤ
ENDO TOSHIYA
遠藤 斗志也 所属 京都産業大学 生命科学部 先端生命科学科 職種 客員教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2010/04 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Structural basis for unfolding pathway-dependent stability of proteins: Vectorial unfolding versus global unfolding |
| 執筆形態 | その他 |
| 掲載誌名 | PROTEIN SCIENCE |
| 出版社・発行元 | JOHN WILEY & SONS INC |
| 巻・号・頁 | 19(4),pp.693-702 |
| 著者・共著者 | Keisuke Yagawa,Koji Yamano,Takaomi Oguro,Masahiro Maeda,Takehiro Sato,Takaki Momose,Shin Kawano,Toshiya Endo |
| 概要 | Point mutations in proteins can have different effects on protein stability depending on the mechanism of unfolding. In the most interesting case of 127, the Ig-like module of the muscle protein titin, one point mutation (Y9P) yields opposite effects on protein stability during denaturant-induced "global unfolding" versus "vectorial unfolding" by mechanical pulling force or cellular unfolding systems. Here, we assessed the reason for the different effects of the Y9P mutation of 127 on the overall molecular stability and N-terminal unraveling by NMR. We found that the Y9P mutation causes a conformational change that is transmitted through beta-sheet structures to reach the central hydrophobic core in the interior and alters its accessibility to bulk solvent, which leads to destabilization of the hydrophobic core. On the other hand, the Y9P mutation causes a bend in the backbone structure, which leads to the formation of a more stable N-terminal structure probably through enhanced hydrophobic interactions. |
| DOI | 10.1002/pro.346 |
| ISSN | 0961-8368 |