Reversible mechanical unfolding of single ubiquitin molecules.

ABSTRACT: Single-molecule manipulation techniques have enabled the characterization of the unfolding and refolding process of individual protein molecules, using mechanical forces to initiate the unfolding transition. Experimental and computational results following this approach have shed new light on the mechanisms of the mechanical functions of proteins involved in several cellular processes, as well as revealed new information on the protein folding/unfolding free-energy landscapes. To investigate how protein molecules of different folds respond to a stretching force, and to elucidate the effects of solution conditions on the mechanical stability of a protein, we synthesized polymers of the protein ubiquitin and characterized the force-induced unfolding and refolding of individual ubiquitin mole

SUBMITTER: Chyan CL 

PROVIDER: S-EPMC1304909 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature