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Circular Dichroism Spectroscopy of Folding in a Protein Monolayer
Author(s) -
Keegan Neil,
Wright Nicholas G.,
Lakey Jeremy H.
Publication year - 2005
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.200462977
Subject(s) - circular dichroism , monolayer , folding (dsp implementation) , protein folding , chemistry , domain (mathematical analysis) , spectroscopy , aqueous solution , crystallography , materials science , nanotechnology , computer science , physics , biochemistry , mathematics , engineering , quantum mechanics , electrical engineering , mathematical analysis
Thin but not invisible : The single layers of proteins needed for screening arrays and nanostructures can be studied by standard UV circular dichroism methods (see picture: colicin N P‐domain on Au surface). In this way the conformational integrity of immobilized proteins can be measured under aqueous conditions, as is currently possible with their soluble counterparts.