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Equilibrium NMR studies of unfolded and partially folded proteins

Nature Structural Biology volume 5, pages 499–503 (1998)Cite this article

Abstract

Multidimensional NMR studies of proteins in unfolded and partially folded states give unique insights into their structures and dynamics and provide new understanding of protein folding and function.

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Figure 1
Figure 2: 1H-15N HSQC spectra of apomyoglobin at three pHs, illustrating the decrease in resonance dispersion in the 1H dimension as the protein unfolds.
Figure 3: Cα backbone superposition of residues 56–140 of folded staphylococcal nuclease (thick tube) and five structures calculated for the fragment Δ131Δ (thin line).
Figure 4: Schematic diagram illustrating the increasing restriction of backbone flexibility as myoglobin folds to increasingly structured and increasingly compact states, from the acid-unfolded state (Uacid), to the pH 4.1 molten globule state (IMG), to native apomyoglobin (Napo), and finally to fully folded holomyoglobin (Nholo).

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Acknowledgements

We thank D. Eliezer, P. Jennings and S. Cavagnero for assistance with preparation of the figures. This work was supported by grants from the National Institutes of Health.

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Authors and Affiliations

  1. the Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, 92037, California, USA

    H. Jane Dyson & Peter E. Wright

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  1. H. Jane Dyson
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  2. Peter E. Wright
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Correspondence to H. Jane Dyson or Peter E. Wright.

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Dyson, H., Wright, P. Equilibrium NMR studies of unfolded and partially folded proteins. Nat Struct Mol Biol 5 (Suppl 7), 499–503 (1998). https://doi.org/10.1038/739

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