Structural origins of nitroxide side chain dynamics on membrane protein α-helical sites.

ABSTRACT: Understanding the structure and dynamics of membrane proteins in their native, hydrophobic environment is important to understanding how these proteins function. EPR spectroscopy in combination with site-directed spin labeling (SDSL) can measure dynamics and structure of membrane proteins in their native lipid environment; however, until now the dynamics measured have been qualitative due to limited knowledge of the nitroxide spin label's intramolecular motion in the hydrophobic environment. Although several studies have elucidated the structural origins of EPR line shapes of water-soluble proteins, EPR spectra of nitroxide spin-labeled proteins in detergents or lipids have characteristic differences from their water-soluble counterparts, suggesting significant differences in the underlyin

SUBMITTER: Kroncke BM 

PROVIDER: S-EPMC2991438 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature