Protein unfolding and refolding under force: methodologies for nanomechanics.
An increasing number of inter- and intramolecular interactions can nowadays be probed using single-molecule manipulation techniques. Protein unfolding and refolding is the most representative--though complex--of these interactions. Herein, we review the main modes of performing a force unfolding experiment: the velocity clamp and the new force clamp mode. We also compare some of the physical aspects behind the two most frequently used single-molecule manipulation instrumentations: optical tweezers and atomic force microscopes.
Samorì
Bruno
B
Department of Biochemistry G. Moruzzi, University of Bologna, Italy. bruno.samori@unibo.it
Zuccheri
G
G
Baschieri
R
R
D000818:Animals; D001703:Biophysics / Q000379:methods*; D002627:Chemistry, Physical / Q000379:methods*; D064211:Connectin; D004247:DNA / Q000737:chemistry; D018625:Microscopy, Atomic Force; D009124:Muscle Proteins / Q000737:chemistry; D009218:Myosins / Q000737:chemistry; D036103:Nanotechnology / Q000379:methods*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry; D013314:Stress, Mechanical
D064211:Connectin; D009124:Muscle Proteins; D011506:Proteins; D004247:DNA; D011494:Protein Kinases; D009218:Myosins