Line narrowing in spectra of proteins dissolved in a dilute liquid crystalline phase by band-selective adiabatic decoupling: application to 1HN-15N residual dipolar coupling measurements.
Residual heteronuclear dipolar couplings obtained from partially oriented protein samples can provide unique NMR constraints for protein structure determination. However, partial orientation of protein samples also causes severe 1H line broadening resulting from residual 1H-1H dipolar couplings. In this communication we show that band-selective 1H homonuclear decoupling during data acquisition is an efficient way to suppress residual 1H-1H dipolar couplings, resulting in spectra that are still amenable to solution NMR analysis, even with high degrees of alignment. As an example, we present a novel experiment with improved sensitivity for the measurement of one-bond 1HN-15N residual dipolar couplings in a protein sample dissolved in magnetically aligned liquid crystalline bicelles.
Vander Kooi
C W
CW
Department of Chemistry, University of Michigan, Ann Arbor 48109, USA.
Kupce
E
E
Zuiderweg
E R
ER
Pellecchia
M
M
D016880:Anisotropy; D003460:Crystallization; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry; D009038:Motion; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D012996:Solutions
D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D011506:Proteins; D012996:Solutions; C063842:dnaK protein, E coli