Open AccessComplete Assignment of the 1 H NMR Spectrum of the Aromatic Residues of Lysozyme
Author(s) -
REDFIELD Christina,
POULSEN Flemming M.,
DOBSON Christopher M.
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06997.x
Subject(s) - chemistry , lysozyme , chemical shift , decoupling (probability) , nuclear magnetic resonance , spectral line , nmr spectra database , nuclear overhauser effect , aromatic amino acids , resonance (particle physics) , nuclear magnetic resonance spectroscopy , two dimensional nuclear magnetic resonance spectroscopy , amino acid , stereochemistry , physics , atomic physics , biochemistry , control engineering , astronomy , engineering
Assignment of the nuclear magnetic resonance (NMR) spectrum of the 59 non‐exchangeable protons of the 13 aromatic amino acid residues of lysozyme has been completed using a combination of selective spin decoupling and nuclear Overhauser experiments. The experimental chemical shift data were used to simulate the aromatic region of the NMR spectrum at 300 MHz and at 470 MHz. Excellent agreement with the experimental spectra was obtained and the simulations permitted more accurate chemical shift values and resonance linewidths to be obtained. The current set of assignments is compared with those of the assignments made previously. Evidence for the motional behaviour of the aromatic amino acid side chains is presented.