Abstract
The interactions of bovine
myelin basic protein with bovine brain GM1 ganglioside
and with lysophosphatidylcholine have been followed
by 1H and 31P N.M.R. The effect of the binding of lipid
on the protein spectrum could be followed in methyl peaks due to methionine and NG-methylarginine
and in peaks from aromatic side chains. Both lipids caused broadening of methyl
resonances from methionine-20, the unique NG-methylarginine
and phenylalanines. The N.M.R. spectral changes on
interaction of peptides derived from N-terminal and C-terminal halves of the
protein with lysolecithin indicated that the lipid
binding was associated with conformational changes involving the central
regions of the polypeptide chain and the methylarginine
residue. The 31P spectra suggest that the average phosphate group in lysophosphatidylcholine becomes more mobile as a result of
binding of basic protein to the lipid micelle.
Cited by
33 articles.
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