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Functional Assays of Membrane‐Bound Proteins with SAMDI‐TOF Mass Spectrometry
Author(s) -
Marin Violeta L.,
Bayburt Timothy H.,
Sligar Stephen G.,
Mrksich Milan
Publication year - 2007
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.200702694
Subject(s) - nanodisc , rhodopsin , mass spectrometry , chemistry , transducin , membrane protein , membrane , biochip , integral membrane protein , biophysics , chromatography , biochemistry , nanotechnology , biology , retinal , materials science
Delicate probing : When nanodisc assemblies are used to present membrane proteins on a biochip surface, interactions of these proteins can be studied by mass spectrometry. The method is illustrated with the protein rhodopsin, which is immobilized to a self‐assembled monolayer by way of a his‐tagged membrane scaffold protein. Upon activation of rhodopsin with light, the protein complex transducin binds and can be detected using SAMDI mass spectrometry.