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

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)179-185
Number of pages7
JournalFEBS Letters
Volume226
Issue number1
DOIs
Publication statusPublished - 21 Dec 1987

Keywords

  • (Horse)
  • Cytochrome c
  • Hyperfine shift
  • Nuclear Overhauser effect
  • Proton NMR
  • Saturation transfer

Fingerprint

Dive into the research topics of 'Proton NMR studies of horse ferricytochrome c Completion of the assignment of the well resolved hyperfine shifted resonances'. Together they form a unique fingerprint.

Cite this