期刊
SCIENCE
卷 335, 期 6066, 页码 319-324出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1214824
关键词
-
资金
- National Cancer Institute of the NIH [R01 CA133592-01, T32CA009054]
- NSF [DMR-0801271, ECCS-0802077]
- NSF (Center for Chemical Innovation on Chemistry at the Space-Time Limit) [CHE-0802913]
- Directorate For Engineering [0802077] Funding Source: National Science Foundation
- Div Of Electrical, Commun & Cyber Sys [0802077] Funding Source: National Science Foundation
Tethering a single lysozyme molecule to a carbon nanotube field-effect transistor produced a stable, high-bandwidth transducer for protein motion. Electronic monitoring during 10-minute periods extended well beyond the limitations of fluorescence techniques to uncover dynamic disorder within a single molecule and establish lysozyme as a processive enzyme. On average, 100 chemical bonds are processively hydrolyzed, at 15-hertz rates, before lysozyme returns to its nonproductive, 330-hertz hinge motion. Statistical analysis differentiated single-step hinge closure from enzyme opening, which requires two steps. Seven independent time scales governing lysozyme's activity were observed. The pH dependence of lysozyme activity arises not from changes to its processive kinetics but rather from increasing time spent in either nonproductive rapid motions or an inactive, closed conformation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据