title: The study of protein mechanics with the atomic force microscope.
abstract: The unfolding and folding of single protein molecules can be studied with an atomic force microscope (AFM). Many proteins with mechanical functions contain multiple, individually folded domains with similar structures. Protein engineering techniques have enabled the construction and expression of recombinant proteins that contain multiple copies of identical domains. Thus, the AFM in combination with protein engineering has enabled the kinetic analysis of the force-induced unfolding and refolding of individual domains as well as the study of the determinants of mechanical stability.
authors.affiliation: Dept of Physiology and Biophysics, Mayo Foundation, 1-117 Medical Sciences Building, Rochester, MN 55905, USA.
authors.forename: T E
authors.initials: TE
authors.lastname: Fisher
authors.forename: A F
authors.initials: AF
authors.lastname: Oberhauser
authors.forename: M
authors.initials: M
authors.lastname: Carrion-Vazquez
authors.forename: P E
authors.initials: PE
authors.lastname: Marszalek
authors.forename: J M
authors.initials: JM
authors.lastname: Fernandez
mesh_terms: D019277:Entropy; D007700:Kinetics; D018625:Microscopy, Atomic Force; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins