Solution NMR investigation of the response of the lactose repressor core domain dimer to hydrostatic pressure.

ABSTRACT: Previous investigations of the sensitivity of the lac repressor to high-hydrostatic pressure have led to varying conclusions. Here high-pressure solution NMR spectroscopy is used to provide an atomic level view of the pressure induced structural transition of the lactose repressor regulatory domain (LacI* RD) bound to the ligand IPTG. As the pressure is raised from ambient to 3kbar the native state of the protein is converted to a partially unfolded form. Estimates of rotational correlation times using transverse optimized relaxation indicates that a monomeric state is never reached and that the predominate form of the LacI* RD is dimeric throughout this pressure change. Spectral analysis suggests that the pressure-induced transition is localized and is associated with a volume change of a

SUBMITTER: Fuglestad B 

PROVIDER: S-EPMC5568981 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature