Unequivocal single-molecule force spectroscopy of proteins by AFM using pFS vectors.

ABSTRACT: Nanomechanical analysis of proteins by single-molecule force spectroscopy based on atomic force microscopy is increasingly being used to investigate the inner workings of mechanical proteins and substrate proteins of unfoldase machines as well as to gain new insight into the process of protein folding. However, such studies are hindered by a number of technical problems, including the noise of the proximal region, ambiguous single-molecule identification, as well as difficulties in protein expression/folding and full-length purification. To overcome these major drawbacks in protein nanomechanics, we designed a family of cloning/expression vectors, termed pFS (plasmid for force spectroscopy), that essentially has an unstructured region to surmount the noisy proximal region, a homomeric poly

SUBMITTER: Oroz J 

PROVIDER: S-EPMC3274811 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature