title: Atomic force microscopy and spectroscopy to probe single membrane proteins in lipid bilayers.
abstract: The atomic force microscope (AFM) has opened vast avenues hitherto inaccessible to the biological scientist. The high temporal (millisecond) and spatial (nanometer) resolutions of the AFM are suited for studying many biological processes in their native conditions. The AFM cantilever stylus is aptly termed as a "lab on a tip" owing to its versatility as an imaging tool as well as a handle to manipulate single bonds and proteins. Recent examples assert that the AFM can be used to study the mechanical properties and monitor processes of single proteins and single cells, thus affording insight into important mechanistic details. This chapter specifically focuses on practical and analytical protocols of single-molecule AFM methodologies related to high-resolution imaging and single-molecule force spectroscopy of membrane proteins. Both these techniques are operator oriented, and require specialized working knowledge of the instrument, theoretical, and practical skills.
authors: Department of Chemistry, University of Oxford, Oxford, UK. tanuj.sapra@chem.ox.ac.uk
authors: K Tanuj
authors: KT
authors: Sapra
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D019617:Halobacterium salinarum / Q000378:metabolism; D021621:Imaging, Three-Dimensional; D008051:Lipid Bilayers / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism* / Q000648:ultrastructure; D018625:Microscopy, Atomic Force / Q000379:methods*; D058767:Protein Unfolding; D013057:Spectrum Analysis / Q000379:methods*; D013816:Thermodynamics
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins; D001436:Bacteriorhodopsins