NMR studies of myelin basic protein. XIII. Assignment of histidine residues in rabbit, bovine and porcine proteins.
Myelin basic protein from three species (rabbit, cow and pig) and peptides from enzymatic digests or cleavage of the proteins have been examined in aqueous solutions by proton nuclear magnetic resonance (NMR) at 400 MHz. The epsilon 1-CH and delta 2-CH resonances of all the histidine residues in the three proteins have been assigned and the pK values have been measured. The heterogeneity of chemical shifts among these resonances can be variously ascribed to persistent localized secondary structures and to effects arising from charged side-chains, particularly those of aspartic acid residues, and from side-chains of aromatic moieties.
G L
GL
Mendz
W J
WJ
Moore
R E
RE
Martenson
D000818:Animals; D002417:Cattle; D006639:Histidine; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D004676:Myelin Basic Protein; D010446:Peptide Fragments; D011489:Protein Denaturation; D011817:Rabbits; D012996:Solutions; D013552:Swine; D014508:Urea
D004676:Myelin Basic Protein; D010446:Peptide Fragments; D012996:Solutions; D006639:Histidine; D014508:Urea