Communication

Stochastic Detection of Monovalent and Bivalent Protein–Ligand Interactions†

  1. Stefan Howorka Dr.1,3,
  2. Joonwoo Nam2,
  3. Hagan Bayley Prof.1,4,
  4. Daniel Kahne Prof.2

Article first published online: 2 FEB 2004

DOI: 10.1002/anie.200352614

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 43, Issue 7, pages 842–846, February 6, 2004

Additional Information

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

Author Information

  1. 1

    The Texas A&M University System Health Science Center, Department of Medical Biochemistry & Genetics, 440 Reynolds Medical Building, College Station, TX 77843-1114, USA

  2. 2

    Department of Chemistry, Princeton University, Princeton, NJ 08544, USA

  3. 3

    Present address: Upper Austrian Research GmbH, Scharitzerstrasse 6–8/4, A-4020, Austria, Fax: (+43) 732-6060-7930

  4. 4

    Present addresses: Department of Chemistry, Texas A&M University, College Station, TX 77843-3255, and, Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, England, UK

  1. †

    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.

Publication History

  1. Issue published online: 2 FEB 2004
  2. Article first published online: 2 FEB 2004
  3. Manuscript Received: 11 AUG 2003

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

View Full Article with Supporting Information (HTML) Get PDF (139K)

Keywords:

  • carbohydrates;
  • molecular recognition;
  • polyvalency;
  • protein engineering;
  • single-molecule studies
Thumbnail image of graphical abstract

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.

View Full Article with Supporting Information (HTML) Get PDF (139K)