title: Protein Backbone 1H(N)-13Calpha and 15N-13Calpha residual dipolar and J couplings: new constraints for NMR structure determination.
abstract: A simple, sensitivity-enhanced experiment was devised for accurate measurement of backbone 15N-13Calpha and 1HN-13Calpha couplings in proteins. The measured residual dipolar couplings 2DHCA, 1DNCA, 3DHCA, and 2DNCA for protein GB1 display very good agreement with the refined NMR structure (PDB code: 3GB1). A Karplus-type relationship between the one-bond 1JNCA couplings and the backbone dihedral psi angles holds, and on the basis of the two-bond 2JNCA couplings a secondary structure index can be established.
authors.affiliation: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
authors.forename: Keyang
authors.initials: K
authors.lastname: Ding
authors.forename: Angela M
authors.initials: AM
authors.lastname: Gronenborn
mesh_terms: D000465:Algorithms; D025561:Bacteriophage Pf1; D009682:Magnetic Resonance Spectroscopy; D019151:Peptide Library; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D019151:Peptide Library; D011506:Proteins