Sequence‐specific assignments of downfield‐shifted amide proton resonances of calmodulin Use of two‐dimensional NMR analysis of its tryptic fragments

FEBS Letters

Hikichi, Kunio¹  Yagi, Koichi¹  Minowa, Osamu¹  Ikura, Mitsuhiko¹  Yazawa, Michio¹ 

[1] High-Resolution Nuclear Magnetic Resonance Laboratory and Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 060, Japan

关键词: Calmodulin;    1H-NMR;    2D NMR;    Hydrogen bonding;   

DOI  :  10.1016/0014-5793(87)81182-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two-dimensional NMR methods were applied to assign the extremely downfield-shifted amide-proton resonances in the 500-MHz ¹H-NMR spectra of the NH₂-terminal fragment of residues 1–75 of calmodulin. The low-field resonances of the ¹H-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 Ca²⁺-free and Ca²⁺-bound states. The hydrogen bonding of glycine residues connecting the two amino acid residues at the Z and − Y positions in the octahedral Ca²⁺ 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.

【 授权许可】

Unknown