High field proton NMR studies of tryptic fragments of calmodulin: a comparison with the native protein.
Addition of the 600 MHz proton magnetic resonance (PMR) spectra of two calmodulin tryptic fragments, residues 1-77 and 78-148, both in the apo- and calcium-bound forms, yielded, to a first order, the corresponding spectrum of intact apo- and calcium-bound calmodulin, respectively. This plus additional data permitted: 1) assignments of resonances to a particular sequence 2) the hypothesis that the secondary and tertiary structures and the calcium binding properties are similar in the fragments and intact calmodulin 3) assignment of the two high affinity calcium sites to the sequence 78-148.
D000818:Animals; D001059:Apoproteins; D002118:Calcium / Q000032:analysis*; D002147:Calmodulin; D002417:Cattle; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008297:Male; D010446:Peptide Fragments / Q000032:analysis; D013737:Testis; D014357:Trypsin
D001059:Apoproteins; D002147:Calmodulin; D010446:Peptide Fragments; D014357:Trypsin; D002118:Calcium