High-pressure EPR spectroscopy studies of the E. coli lipopolysaccharide transport proteins LptA and LptC.

ABSTRACT: The use of pressure is an advantageous approach to the study of protein structure and dynamics because it can shift the equilibrium populations of protein conformations toward higher energy states that are not of sufficient population to be observable at atmospheric pressure. Recently, the Hubbell group at the University of California, Los Angeles, reintroduced the application of high pressure to the study of proteins by electron paramagnetic resonance (EPR) spectroscopy. This methodology is possible using X-band EPR spectroscopy due to advances in pressure intensifiers, sample cells, and resonators. In addition to the commercial availability of the pressure generation and sample cells by Pressure Biosciences Inc., a five-loop-four-gap resonator required for the initial high pressure EPR s

SUBMITTER: Schultz KM 

PROVIDER: S-EPMC5761346 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature