Mixing and Matching Detergents for Membrane Protein NMR Structure Determination

Journal Article · Wed Oct 21 00:00:00 EDT 2009 · J. Am. Chem. Soc.

DOI:https://doi.org/10.1021/ja808776j· OSTI ID:1005636

Columbus, Linda; Lipfert, Jan; Jambunathan, Kalyani; Fox, Daniel A; Sim, Adelene Y.L.; Doniach, Sebastian; Lesley, Scott A

One major obstacle to membrane protein structure determination is the selection of a detergent micelle that mimics the native lipid bilayer. Currently, detergents are selected by exhaustive screening because the effects of protein-detergent interactions on protein structure are poorly understood. In this study, the structure and dynamics of an integral membrane protein in different detergents is investigated by nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy and small-angle X-ray scattering (SAXS). The results suggest that matching of the micelle dimensions to the protein's hydrophobic surface avoids exchange processes that reduce the completeness of the NMR observations. Based on these dimensions, several mixed micelles were designed that improved the completeness of NMR observations. These findings provide a basis for the rational design of mixed micelles that may advance membrane protein structure determination by NMR.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States)
• Sponsoring Organization: USDOE
• OSTI ID: 1005636
• Journal Information: J. Am. Chem. Soc., Vol. 131, Issue (21) ; 06, 2009; ISSN 0002-7863
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
DETERGENTS
DIMENSIONS
DYNAMICS
ELECTRON SPIN RESONANCE
INTEGRALS
INTERACTIONS
LIPIDS
MEMBRANE PROTEINS
MIXING
NUCLEAR MAGNETIC RESONANCE
PROTEIN STRUCTURE
SMALL ANGLE SCATTERING
SCREENING
SPECTROSCOPY
SURFACES