Solid-state NMR approaches to measure topological equilibria and dynamics of membrane polypeptides.
Biological membranes are characterized by a high degree of dynamics. In order to understand the function of membrane proteins and even more of membrane-associated peptides, these motional aspects have to be taken into consideration. Solid-state NMR spectroscopy is a method of choice when characterizing topological equilibria, molecular motions, lateral and rotational diffusion as well as dynamic oligomerization equilibria within fluid phase lipid bilayers. Here we show and review examples where the (15)N chemical shift anisotropy, dipolar interactions and the deuterium quadrupolar splittings have been used to analyze motions of peptides such as peptaibols, antimicrobial sequences, Vpu, phospholamban or other channel domains. In particular, simulations of (15)N and (2)H-solid-state NMR spectra are shown of helical domains in uniaxially oriented membranes when rotation around the membrane normal or the helix long axis occurs.
Salnikov
Evgeniy
E
Université de Strasbourg / CNRS, UMR7177, Institut de chimie, 4, rue Blaise Pascal, 67070 Strasbourg, France.
Aisenbrey
Christopher
C
Vidovic
Verica
V
Bechinger
Burkhard
B
D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017433:Protein Structure, Secondary / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology
D008565:Membrane Proteins