Resonance assignment strategies for the analysis of nmr spectra of proteins |
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Authors: | M F Leopold Jeffrey L Urbauer A Joshua Wand |
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Institution: | (1) Department of Biochemistry, University of Illinois, Champaign-Urbana, RAL 493, Box B-4, 61801 Urbana, IL |
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Abstract: | Determination of the high resolution solution structure of a protein using nuclear magnetic resonance (NMR) spectroscopy requires
that resonances observed in the NMR spectra be unequivocally assigned to individual nuclei of the protein. With the advent
of modern, two-dimensional NMR techniques arose methodologies for assigning the1H resonances based on 2D, homonuclear1H NMR experiments. These include the sequential assignment strategy and the main chain directed strategy. These basic strategies
have been extended to include newer 3D homonuclear experiments and 2D and 3D heteronuclear resolved and edited methods. Most
recently a novel, conceptually new approach to the problem has been introduced that relies on heteronuclear, multidimensional
so-called triple resonance experiments for both backbone and sidechain resonance assignments in proteins. This article reviews
the evolution of strategies for the assignment of resonances of proteins. |
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Keywords: | NMR spectroscopy resonances of proteins resonance assignment strategies |
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