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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. © 1980.

Original publication

DOI

10.1016/0022-2364(80)90099-2

Type

Journal article

Journal

Journal of Magnetic Resonance (1969)

Publication Date

15/01/1980

Volume

37

Pages

141 - 153