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Biosynthetic Incorporation of 15N and 13C for Assignment and Interpretation of Nuclear Magnetic Resonance Spectra of Proteins

Published online by Cambridge University Press:  17 March 2009

Lawrence P. McIntosh  and
Frederick W. Dahlquist
Lawrence P. McIntosh
Affiliation:
Department of Chemistry and Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA
Frederick W. Dahlquist
Affiliation:
Department of Chemistry and Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA
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The use of isotopic substitution is a time-honoured method for simplifying the nuclear magnetic resonance spectra of biological macromolecules. For example, the biosynthetic incorporation of a heteronucleus such as 15N or 13C into a specific amino acid residue in a protein followed by direct observation of the 15N or 13C NMR spectrum could provide a means to specifically observe a given amino acid type in that protein. By observation of the chemical shift or relaxation properties as a function of pH, ligand concentration, etc. a number of important conclusions concerning the pKa values of specific residues, the affinity of the protein for various ligands, or dynamic properties of the protein can be deduced. (See Henry et al. 1986 a, b; 1987 for an elegant modern example). In such situations, direct observation of the heteronucleus is a powerful means to observe environmental changes (Niu et al. 1979) but often these measurements are not readily interpretable in terms of alterations of protein structure. Although proton-proton dipolar interactions (NOEs) typically provide the richest source of such structural information, these interactions are not monitored in most experiments which directly observe the heteronucleus.

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Research Article
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Quarterly Reviews of Biophysics , Volume 23 , Issue 1 , February 1990 , pp. 1 - 38
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Copyright © Cambridge University Press 1990

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