Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces.

ABSTRACT: Knowing the topology and location of protein segments at water-membrane interfaces is critical for rationalizing their functions, but their characterization is challenging under physiological conditions. Here, we debut a unique spectroscopic approach by using the hydration dynamics gradient found across the phospholipid bilayer as an intrinsic ruler for determining the topology, immersion depth, and orientation of protein segments in lipid membranes, particularly at water-membrane interfaces. This is achieved through the site-specific quantification of translational diffusion of hydration water using an emerging tool, (1)H Overhauser dynamic nuclear polarization (ODNP)-enhanced NMR relaxometry. ODNP confirms that the membrane-bound region of α-synuclein (αS), an amyloid protein known to in

SUBMITTER: Cheng CY 

PROVIDER: S-EPMC3800990 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature