Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm.

ABSTRACT: Thermodynamic stabilities are pivotal for understanding structure-function relationships of proteins, and yet such determinations are rare for membrane proteins. Moreover, the few measurements that are available have been conducted under very different experimental conditions, which compromises a straightforward extraction of physical principles underlying stability differences. Here, we have overcome this obstacle and provided structure-stability comparisons for multiple membrane proteins. This was enabled by measurements of the free energies of folding and the m values for the transmembrane proteins PhoP/PhoQ-activated gene product (PagP) and outer membrane protein W (OmpW) from Escherichia coli. Our data were collected in the same lipid bilayer and buffer system we previously used to de

SUBMITTER: Moon CP 

PROVIDER: S-EPMC3600475 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature