15N chemical shift anisotropy in protein structure refinement and comparison with NH residual dipolar couplings.
Recent methods of aligning proteins which were developed in order to measure residual dipolar couplings (RDCs) in solution can also be used for additional applications such as measuring the 15N CSA in the form of chemical shift differences, Deltadelta. A new XPLOR-NIH module has been developed and implemented for NMR structure refinement using the 15N Deltadelta data as restraints. The results of this refinement are shown using the protein Bax. This method should be amenable to any protein which can be studied by NMR. An analysis comparing the structural information provided by NH RDCs and the 15N Deltadelta is included.
Lipsitz
Rebecca S
RS
Laboratory of Biophysical Chemistry, Building 50, Room 3503, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892-8013, USA.
Tjandra
Nico
N
D000465:Algorithms; D016880:Anisotropy; D003198:Computer Simulation; D006859:Hydrogen / Q000737:chemistry; D006860:Hydrogen Bonding; D008280:Magnetics; D008958:Models, Molecular; D009587:Nitrogen Isotopes / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D011518:Proto-Oncogene Proteins / Q000737:chemistry; D019253:Proto-Oncogene Proteins c-bcl-2; D011786:Quality Control; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity; D051028:bcl-2-Associated X Protein
D009587:Nitrogen Isotopes; D011506:Proteins; D011518:Proto-Oncogene Proteins; D019253:Proto-Oncogene Proteins c-bcl-2; D051028:bcl-2-Associated X Protein; D006859:Hydrogen