Proton NMR studies of horse ferricytochrome c Completion of the assignment of the well resolved hyperfine shifted resonances

FEBS Letters

Turner, David L.¹  Santos, Helena¹ 

[1] Centro de Quimica Estrutural, UNL,Av. Rovisco Pais, 1000 Lisboa, Portugal

关键词: Cytochrome c;    Proton NMR;    Hyperfine shift;    Nuclear Overhauser effect;    Saturation transfer;    (Horse);   

DOI  :  10.1016/0014-5793(87)80575-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

¹H NMR saturation transfer and nuclear Overhauser effect (NOE) measurements have been used together with two-dimensional spectra to complete the assignment of the well resolved hyperfine shifted resonances in the spectrum of horse ferricytochrome c and obtain their shifts in the reduced protein. New assignments include the β-CH₂ protons of Met-80, both ring protons of His-18, and the α-CH₂ of Gly-29 and δ-CH₂ of Pro-30, which resonate surprisingly far upfield despite the absence of any Fermi contact contribution to the shift.

【 授权许可】

Unknown