title: Calcium-binding proteins afford calibration of dihedral-angle dependence of 3J(NC(gamma)) coupling constant in aspartate and asparagine residues.
abstract: Calibration of the 3J(NC(gamma)) couplings across the N-C(alpha)-C(beta)-C(gamma) fragment of aspartate and asparagine residues is afforded by two interactions that produce fixed conformations of the side chains in solution. One is the binding of these side chains to calcium ions; the other is the H-bond interaction of these side chains with a backbone amide.
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, MN 55905, USA. juranic.nenad@mayo.edu
authors.forename: Nenad
authors.initials: N
authors.lastname: Juranić
authors.forename: Elena
authors.initials: E
authors.lastname: Atanasova
authors.forename: Martin C
authors.initials: MC
authors.lastname: Moncrieffe
authors.forename: Franklyn G
authors.initials: FG
authors.lastname: Prendergast
authors.forename: Slobodan
authors.initials: S
authors.lastname: Macura
mesh_terms: D001216:Asparagine / Q000737:chemistry*; D001224:Aspartic Acid / Q000737:chemistry*; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002138:Calibration; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation
chemical_list: D002135:Calcium-Binding Proteins; D001224:Aspartic Acid; D001216:Asparagine