蛋白質の構�?�予測と安定化のための技術の検証

Chem-Bio Informatics Journal

村�?? 匡⁴  皆川 宏貴⁵  島田 次郎⁵  山岸 良介¹  大西 楢平³  水野 洋²  石井 元⁴  金子 寛生¹  八木 博隆⁴  古市 真木雄⁴ 

[1] 日本大学�?文理学部�?物理生命システム科学科;独立行政法人産業�?術総合研究所;東邦大学�?理学部;NECソフト株式会社�??VALWAYテクノロジーセンター;日本電気株式会社�? ナノエレクトロニクス研究�?

关键词: homology modeling;    ホモロジーモデリング;    thermostability;    熱安定�?�;    TIM barrel;    TIMバレル;    lactate oxidase;    乳酸酸化酵素;    protein engineering;    蛋白質工学;    biosensor;    バイオセンサー;    computer-aided design;    コンピュータ支援による分子設計;   

DOI  :  10.1273/cbij.9.62

学科分类：生物化学/生物物理

来源: Chem-Bio Informatics Society

【 摘 要 】

References(27)Recently, a variety of methods for protein structure prediction have been developed. However, there are only a limited number of studies where the results have been adequately validated. With this in mind, we have evaluated our previously predicted model of lactate oxidase by comparison with the recently determined crystal structure. In addition, we also analyzed our thermotolerant mutants that were designed on the basis of a predicted model.The validity of these procedures was assessed by comparing the results of rational design against the interpretation of the thermostabilization mechanism. Specifically, we analyzed lactate oxidase (LOX), a useful lactic acid sensor, as an example for validation.LOX was chosen because it has an (β/α)8 barrel (TIM barrel) fold, which constitutes the basic structural framework of numerous important enzymes. We also propose an effective modeling method and thermostabilization technique for the TIM barrel fold.

【 授权许可】

Unknown