Premium
Proton NMR studies of horse ferricytochrome c Completion of the assignment of the well resolved hyperfine shifted resonances
Author(s) -
Santos Helena,
Turner David L.
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)80575-6
Subject(s) - hyperfine structure , chemistry , proton , fermi contact interaction , nuclear magnetic resonance , spectral line , proton nmr , atomic physics , crystallography , stereochemistry , physics , nuclear physics , astronomy
1 H 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‐CH 2 protons of Met‐80, both ring protons of His‐18, and the α‐CH 2 of Gly‐29 and δ‐CH 2 of Pro‐30, which resonate surprisingly far upfield despite the absence of any Fermi contact contribution to the shift.