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Transverse relaxation effects resulting from deuterium exchange in the proton NMR spectra of proteins

1980; Elsevier BV; Volume: 37; Issue: 1 Linguagem: Inglês

10.1016/0022-2364(80)90099-2

1557-8968

Robert Cassels, Christopher M. Dobson, Flemming M. Poulsen, R. George Ratcliffe, Robert J. P. Williams,

Molecular spectroscopy and chirality

The exchange of the NIH hydrogen of tryptophan for deuterium is shown to cause significant changes in the proton relaxation behavior of the C2H hydrogen, both in the free amino acid and in the protein lysozyme. In lysozyme, the transverse relaxation behavior is monitored with a spin-echo method and, in conjunction with a nuclear Overhauser measurement, this is used to complete the identification of the tryptophan N1H resonances from the different residues. The observed changes in relaxation times are shown to be consistent with the expected rotational correlation times.