动力学
脂肪酶
化学
酶动力学
水解
催化作用
酶
基质(水族馆)
共焦
酶催化
共焦显微镜
有机化学
物理
活动站点
光学
生物
生态学
量子力学
作者
Kelly Velonia,Ophir Flomenbom,Davey Loos,Sadahiro Masuo,Mircea Cotlet,Yves Engelborghs,Johan Hofkens,Alan E. Rowan,J. Klafter,Roeland J. M. Nolte,Frans C. De Schryver
标识
DOI:10.1002/anie.200460625
摘要
Real-time measurement of the catalysis and substrate kinetics of a single-enzyme hydrolysis reaction is demonstrated with confocal fluorescence microscopy (CFM; see picture, green=CFM beam). A single lipase is shown to have a broad range of conformations; each conformation contributes to the overall enzymatic activity, an observation that is often masked by ensemble measurements. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2005/z460625_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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