Calcium-binding proteins afford calibration of dihedral-angle dependence of 3J(NC(gamma)) coupling constant in aspartate and asparagine residues.
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.
Juranić
Nenad
N
Department of Biochemistry and Molecular Biology, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, MN 55905, USA. juranic.nenad@mayo.edu
Atanasova
Elena
E
Moncrieffe
Martin C
MC
Prendergast
Franklyn G
FG
Macura
Slobodan
S
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
D002135:Calcium-Binding Proteins; D001224:Aspartic Acid; D001216:Asparagine