Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening.
We demonstrate that a significant improvement in the spectral resolution may be achieved in solid-state NMR experiments of proteins in inhomogeneously disordered oriented lipid bilayers. Using 1H homonuclear decoupling instead of standard 1H heteronuclear decoupling, the 15N line widths may be reduced by up to seven times for such samples. For large oriented membrane proteins, such resolution enhancements may be crucial for assignment and structural interpretation.
Vosegaard
Thomas
T
Center for Insoluble Protein Structures and Department of Chemistry, University of Aarhus, Langelandsgade 140, DK-8000 Aarhus C, Denmark. tv@chem.au.dk
Bertelsen
Kresten
K
Pedersen
Jan M
JM
Thøgersen
Lea
L
Schiøtt
Birgit
B
Tajkhorshid
Emad
E
Skrydstrup
Troels
T
Nielsen
Niels Chr
NC
D008565:Membrane Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D013816:Thermodynamics
D008565:Membrane Proteins