Stretching single molecules into novel conformations using the atomic force microscope.
A dense network of interconnected proteins and carbohydrates forms the complex mechanical scaffold of living tissues. The recently developed technique of single molecule force spectroscopy using the atomic force microscope (AFM) has enabled a detailed analysis of the force-induced conformations of these molecules and the determinants of their mechanical stability. These studies provide some of the basic knowledge required to understand the mechanical interactions that define all biological organisms.
Fisher
T E
TE
Department of Physiology and Biophysics, Mayo Foundation, 1-117 Medical Sciences Building, Rochester, Minnesota 55905, USA.
Marszalek
P E
PE
Fernandez
J M
JM
D000818:Animals; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D018625:Microscopy, Atomic Force / Q000379:methods*; D016296:Mutagenesis / Q000235:genetics; D020815:Polyproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D020673:Protein Renaturation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013314:Stress, Mechanical
D020815:Polyproteins; D011134:Polysaccharides; D011506:Proteins; D011993:Recombinant Fusion Proteins; D004247:DNA