Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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




Journal article


Journal of Magnetic Resonance (1969)

Publication Date





141 - 153