Stochastic detection of monovalent and bivalent protein-ligand interactions

被引：80
作者：
Howorka, S
Nam, J
Bayley, H
Kahne, D
机构：
[1] Texas A&M Univ Syst Hlth Sci Ctr, Dept Med Biochem & Genet, College Stn, TX 77843 USA
[2] Princeton Univ, Dept Chem, Princeton, NJ 08544 USA
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2004年 / 43卷 / 07期
关键词：
carbohydrates; molecular recognition; polyvalency; protein engineering; single-molecule studies;
D O I：
10.1002/anie.200352614
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Single-molecule study on multivalency: The binding kinetics of a tetravalent lectin can be examined at the single-molecule level by using an engineered protein pore carrying up to seven carbohydrate ligands. The binding of the lectin to the pore (see molecular model) produces short and long reversible blockades in single-channel current recordings, which are interpreted as monovalent and bivalent binding events, respectively.
引用
收藏
页码：842 / 846
页数：5
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