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Specific Protein Docking to Chelator Lipid Monolayers Monitored by FT‐IR Spectroscopy at the Air–Water Interface
Author(s) -
Schmitt Lutz,
Boha Tom M.,
Denzinger Steffen,
Ringsdorf Helmut,
Tampé Robert
Publication year - 1996
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199603171
Subject(s) - chelation , monolayer , chemistry , docking (animal) , spectroscopy , histidine , metal , fusion protein , infrared spectroscopy , materials science , biochemistry , inorganic chemistry , organic chemistry , enzyme , medicine , physics , nursing , quantum mechanics , gene , recombinant dna
A novel class of chelator lipids combines the fundamental properties of self‐assembly with protein engineering techniques, leading to well‐organized biofunctionalized interfaces and two‐dimensional protein arrays. Reflection FT‐IR spectroscopy at the air ‐ water interface was used to monitor the formation of a metal‐sensitive lipid film as well as the reversible and specific docking (represented on the right) of a fusion protein (B) to this chelator lipid layer through a histidine tag (A).