Sensitivity-enhanced 2D IPAP, TROSY-anti-TROSY, and E.COSY experiments: alternatives for measuring dipolar 15N-1HN couplings.
Sensitivity-enhanced versions of the IPAP, TROSY-anti-TROSY, and E.COSY experiments for measuring one-bond 15N-1HN couplings are presented. Together with the previously developed sensitivity-enhanced E.COSY-type HSQC experiment they comprise a suite of sensitivity-enhanced experiments that allows one to chose the optimal spectrum for accurate measurement of one-bond 15N-1HN residual dipolar couplings in proteins. Since one-bond 15N-1HN residual dipolar couplings play uniquely important roles in structural NMR, these additional methods provide further tools for improving structure determination of proteins and other biological macromolecules.
Ding
Keyang
K
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Building 5, Room 130, Bethesda, MD 20892-0520, USA.
Gronenborn
Angela M
AM
D001426:Bacterial Proteins / Q000737:chemistry*; D008280:Magnetics; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D011522:Protons; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D009587:Nitrogen Isotopes; D011506:Proteins; D011522:Protons