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Sequence‐specific assignments of downfield‐shifted amide proton resonances of calmodulin Use of two‐dimensional NMR analysis of its tryptic fragments
Author(s) -
Ikura Mitsuhiko,
Minowa Osamu,
Yazawa Michio,
Yagi Koichi,
Hikichi Kunio
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81182-1
Subject(s) - chemistry , amide , calmodulin , proton nmr , crystallography , stereochemistry , octahedron , nmr spectra database , proton , amino acid , peptide sequence , amino acid residue , carbon 13 nmr , spectral line , calcium , biochemistry , crystal structure , organic chemistry , physics , quantum mechanics , astronomy , gene
Two‐dimensional NMR methods were applied to assign the extremely downfield‐shifted amide‐proton resonances in the 500‐MHz 1 H‐NMR spectra of the NH 2 ‐terminal fragment of residues 1–75 of calmodulin. The low‐field resonances of the 1 H‐NMR spectra of intact calmodulin were assigned to specific amino acid residues by comparison with spectra of the tryptic fragments of residues 1–75 and 78–148, in both the Ca 2+ ‐free and Ca 2+ ‐bound states. The hydrogen bonding of glycine residues connecting the two amino acid residues at the Z and − Y positions in the octahedral Ca 2+ coordination site was investigated. The Gly 134 in site IV showed a different property from the other glycines, 25, 61 and 98, involved in sites I, II and III, respectively.