Identification of a mechanical rheostat in the hydrophobic core of protein L.

ABSTRACT: The ability of proteins and their complexes to withstand or respond to mechanical stimuli is vital for cells to maintain their structural organisation, to relay external signals and to facilitate unfolding and remodelling. Force spectroscopy using the atomic force microscope allows the behaviour of single protein molecules under an applied extension to be investigated and their mechanical strength to be quantified. protein L, a simple model protein, displays moderate mechanical strength and is thought to unfold by the shearing of two mechanical sub-domains. Here, we investigate the importance of side-chain packing for the mechanical strength of protein L by measuring the mechanical strength of a series of protein L variants containing single conservative hydrophobic volume deletion mutants

SUBMITTER: Sadler DP 

PROVIDER: S-EPMC2796179 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature