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Stochastic Detection of Monovalent and Bivalent Protein–Ligand Interactions
Author(s) -
Howorka Stefan,
Nam Joonwoo,
Bayley Hagan,
Kahne Daniel
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200352614
Subject(s) - bivalent (engine) , chemistry , lectin , biophysics , kinetics , molecule , nanotechnology , computational biology , crystallography , biochemistry , materials science , physics , biology , organic chemistry , quantum mechanics , metal
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.