Dipolar Waves as NMR maps of helices in proteins.
Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a helix and the type of helix, deviations from ideality, and to orient the helices relative to an external axis in completely aligned samples and relative to each other in a common frame in weakly aligned samples with Dipolar Waves. They provide a tool for accurately describing helices and a step towards high throughput structure determination of proteins.
Mesleh
Michael F
MF
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.
Opella
Stanley J
SJ
D000465:Algorithms; D003461:Crystallography / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008280:Magnetics; D009587:Nitrogen Isotopes; D010507:Periodicity; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D013113:Spin Labels
D009587:Nitrogen Isotopes; D011506:Proteins; D011522:Protons; D013113:Spin Labels