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Imaging and Quantifying Chemical and Physical Properties of Native Proteins at Molecular Resolution by Force–Volume AFM
Author(s) -
Medalsy Izhar,
Hensen Ulf,
Muller Daniel J.
Publication year - 2011
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.201103991
Subject(s) - bacteriorhodopsin , atomic force microscopy , resolution (logic) , embedding , volume (thermodynamics) , nanotechnology , anisotropy , proton , high resolution , chemistry , membrane , materials science , computer science , physics , optics , thermodynamics , artificial intelligence , remote sensing , geology , biochemistry , quantum mechanics
Use the force : Force–volume atomic force microscopy (AFM) can image native membrane proteins and quantify and map their chemical and physical properties at molecular resolution (see images). For the light‐driven proton pump bacteriorhodopsin (BR), the data shows that lipids form a flexible framework embedding a mechanically anisotropic proton pump, and that the BR adopts different structurally stable conformations that are important for proton pumping.