
TY  - JOUR
A1  - Littlemore, LAT 
T1  - N.M.R. studies on myelin basic protein. II. <sup>1</sup>H N.M.R. studies of the protein and constituent peptides in aqueous solutions
JF  - Australian Journal of Chemistry
JO  - Aust. J. Chem.
Y1  - 1978
VL  - 31
IS  - 11
SP  - 2387
EP  - 2398
KW  - 
UR  - https://doi.org/10.1071/CH9782387 
N2  - 1H N.M.R. spectra (270 MHz) of myelin basic protein (MBP) at pD 3.7 in D2O were obtained as a function of concentration and compared with computed spectra. Reduced line widths obtained for 0.5-mM samples and use of the convolution difference technique enabled detection of chemical shift heterogeneities for histidine, tyrosine, methionine, threonine, and isoleucine residues in the protein; this is indicative of secondary/tertiary structure. Chemical shift assignments were confirmed by the use of the Carr-Purcell A pulse sequence and selective decoupling as well as by correlation of the MBP spectrum with that of its constituent cathepsin D digest peptides. The methyl resonance from the unique methylated arginine-107 was found, and its chemical shift compared to that of NG-monomethyl-L-arginine and the methylated arginine peak in the peptide fragment, residues 90-170. The absence of ring- current effects on the methyl chemical shift precludes conformations of MBP in which the methylarginine interacts with the phenylalanine pair at residues 89 and 90. 
ER  -

