This work was supported by the U.S. Department of Energy, the DoD Tri-Service Technology Program, the National Institutes of Health, the Office of Naval Research (Multidisciplinary University Research Initiative 1999), and the Texas Advanced Technology Program. H.B. is the holder of a Royal Society-Wolfson Research Merit Award. S.H. held fellowships from the Austrian Science Foundation (Fonds zur Förderung der wissenschaftlichen Forschung) and the Max-Kade Foundation.
Stochastic Detection of Monovalent and Bivalent Protein–Ligand Interactions†
Article first published online: 2 FEB 2004
Copyright © 2004 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 43, Issue 7, pages 842–846, February 6, 2004
How to Cite
Howorka, S., Nam, J., Bayley, H. and Kahne, D. (2004), Stochastic Detection of Monovalent and Bivalent Protein–Ligand Interactions. Angew. Chem. Int. Ed., 43: 842–846. doi: 10.1002/anie.200352614
- Issue published online: 2 FEB 2004
- Article first published online: 2 FEB 2004
- Manuscript Received: 11 AUG 2003
- molecular recognition;
- protein engineering;
- single-molecule studies
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.