Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides under Magic Angle Spinning. The functional dependence of a series of anisotropic recoupling schemes is analyzed using theoretical and numerical methods. These studies lead to the construction of a set of polarization dephasing or transfer units that probe local backbone conformation and overall molecular orientation within the same NMR experiment. Experimental results are shown for a randomly oriented peptide and for two model membrane-peptides reconstituted into lipid bilayers and oriented on polymer films according to a method proposed by Bechinger et al.
Andronesi
O C
OC
Department of NMR-Based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Pfeifer
J R
JR
Al-Momani
L
L
Ozdirekcan
S
S
Rijkers
D T S
DT
Angerstein
B
B
Luca
S
S
Koert
U
U
Killian
J A
JA
Baldus
M
M
D016880:Anisotropy; D006096:Gramicidin / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D013113:Spin Labels
D008051:Lipid Bilayers; D010455:Peptides; D013113:Spin Labels; D006096:Gramicidin