Elimination of cross-relaxation effects from two-dimensional chemical-exchange spectra of macromolecules

J. Fejzo, Slobodan I Macura, S. Macura, J. L. Markley

Research output: Contribution to journalArticle

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Abstract

We demonstrate here a method for eliminating cross-relaxation effects from exchange spectra of macromolecules that permits a more rigorous study of chemical-exchange processes. In the spin diffusion limit, the laboratory-frame cross-relaxation rate is negative and equal to half the rotating-frame cross-relaxation rate, which is positive. If, during the mixing time, the magnetization is flipped rapidly between the two frames such that the average residence time in the NOESY:ROESY frames is 2:1, then the magnetization exchange due to cross-relaxation will cancel out and be removed. Since chemical exchange takes place steadily, irrespective of the frame of reference, it will contribute to cross-peak volumes in the usual manner. This approach has been applied to the elimination of cross-relaxation effects from the 2D exchange spectrum of a small globular protein, turkey ovomucoid third domain (6062 Da). The results demonstrate that tyrosine-31 executes ring flips on the millisecond time scale.

Original languageEnglish (US)
Pages (from-to)2574-2577
Number of pages4
JournalJournal of the American Chemical Society
Volume112
Issue number7
DOIs
StatePublished - 1990
Externally publishedYes

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Macromolecules
Magnetization
Ovomucin
Chemical Phenomena
Tyrosine
Proteins

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Elimination of cross-relaxation effects from two-dimensional chemical-exchange spectra of macromolecules. / Fejzo, J.; Macura, Slobodan I; Macura, S.; Markley, J. L.

In: Journal of the American Chemical Society, Vol. 112, No. 7, 1990, p. 2574-2577.

Research output: Contribution to journalArticle

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