title: Single molecule probing of SNARE proteins by atomic force microscopy.
abstract: Atomic force microscopy (AFM) in force spectroscopy mode has recently emerged as a technique of choice for studying mechanical interactions between the proteins of the core soluble N-ethylmaleimide-sensitive fusion protein attachment protein attachment protein receptor (SNARE) complex. In these experiments, the rupture force, extension, spontaneous dissociation time, and interaction energy for SNARE protein-protein interactions can be obtained at the single molecule level. These measurements, which are complementary to results and conclusions drawn from other techniques, improve our understanding of the role of the SNARE complex in exocytosis.
authors.affiliation: Department of Neurobiology, Center for Glial Biology in Medicine, Atomic Force Microscopy and Nanotechnology Laboratories, Civitan International Research Center, Evelyn F. McKnight Brain Institute, University of Alabama, Birmingham, Alabama 35294, USA.
authors.forename: Wei
authors.initials: W
authors.lastname: Liu
authors.forename: Vladimir
authors.initials: V
authors.lastname: Parpura
mesh_terms: D018625:Microscopy, Atomic Force / Q000295:instrumentation* / Q000379:methods*; D015336:Molecular Probe Techniques / Q000295:instrumentation*; D011485:Protein Binding; D050600:SNARE Proteins / Q000032:analysis* / Q000378:metabolism*
chemical_list: D050600:SNARE Proteins