Probing the mechanical stability of proteins using the atomic force microscope.
The mechanical strength of single protein molecules can be investigated by using the atomic force microscope. By applying this technique to a wide range of proteins, it appears that the type of secondary structure and its orientation relative to the extension points are important determinants of mechanical strength. Unlike chemical denaturants, force acts locally and the mechanical strength of a protein may thus appear to be mechanically weak or strong by simply varying the region of the landscape through which the protein is unfolded. Similarly, the effect of ligand binding on the mechanical resistance of a protein may also depend on the relative locations of the binding site and force application. Mechanical deformation may thus facilitate the degradation or remodelling of thermodynamically stable proteins and their complexes in vivo.
Brockwell
D J
DJ
Institute of Molecular and Cellular Biology and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, U.K. brock@bmbaxp.leeds.ac.uk
D001665:Binding Sites; D008024:Ligands; D018625:Microscopy, Atomic Force / Q000379:methods*; D008958:Models, Molecular; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012680:Sensitivity and Specificity; D013816:Thermodynamics
D008024:Ligands; D011506:Proteins