NMR studies of myelin basic protein. IX. Complete assignments of the tyrosine residues by proton NMR of proteins from six species.
All the proton resonances from the tyrosine residues are assigned in 400 MHz NMR spectra in aqueous solution of myelin basic proteins from human, cow, pig, rabbit, rat (small protein) and chicken. Assignments are based on species comparisons, spectra of enzymatic cleavage products of the basic protein, pH titrations, broadening effects of Gd(III), and nuclear Overhauser effects. The mobile extended polypeptide chain structure of the protein facilitates the detection of interactions between nearest neighbors. Evidence is found for reverse turns in the structure in regions of encephalitogenic determinants.
D000818:Animals; D002417:Cattle; D002645:Chickens; D005682:Gadolinium; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D004676:Myelin Basic Protein; D011487:Protein Conformation; D011817:Rabbits; D051381:Rats; D013045:Species Specificity; D013552:Swine; D014443:Tyrosine
D004676:Myelin Basic Protein; D014443:Tyrosine; D005682:Gadolinium