Abstract
Complete sequence-specific resonance assignments have been determined for a calcium phosphate sequestering, phosphoseryl-containing, tryptic peptide α s1-casein(59–79) containing the phosphorylated motif -SSSEE-. Spectra have been recorded in the presence of excess Ca 2+ and at three different values of sample pH to characterize the changes in peptide conformation as calcium binds to the phosphorylated residues. The secondary structure of the peptide was characterized by sequential ( i,i + 1), medium-range ( i,i + 2/3/4), and long-range ( i,i + 5) NOE connectivities, C αH chemical shifts, NH to C αH coupling constants and the observation of slowly exchanging amide protons. Two structured regions have been identified: residues P73 to V76 implicated in β-turn conformations, and residues E61 to Σ67 involved in a loop-type structure.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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