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Review
. 2009 Feb;19(1):23-30.
doi: 10.1016/j.sbi.2008.12.004. Epub 2009 Jan 21.

Biophysical characterization of intrinsically disordered proteins

David Eliezer  1
Affiliations
Review

Biophysical characterization of intrinsically disordered proteins

David Eliezer. Curr Opin Struct Biol. 2009 Feb.

Abstract

The challenges associated with the structural characterization of disordered proteins have resulted in the application of a host of biophysical methods to such systems. NMR spectroscopy is perhaps the most readily suited technique for providing high-resolution structural information on disordered protein states in solution. Optical methods, solid state NMR, ESR and X-ray scattering can also provide valuable information regarding the ensemble of conformations sampled by disordered states. Finally, computational studies have begun to assume an increasingly important role in interpreting and extending the impact of experimental data obtained for such systems. This article discusses recent advances in the applications of these methods to intrinsically disordered proteins.

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Conflict of interest statement

Conflict of Interest

The author has no conflicts to declare.

Figures

Figure 1
Figure 1. NMR α-carbon secondary chemical shifts and NH RDCs for β-synuclein
Chemical shift deviations from random coil values indicate a preference for extended structure (negative values) in the C-terminal region and helical structure (positive values) in the N-terminal region. Large amplitude RDCs in the C-terminal region correlate qualitatively with negative shift deviations and likely reflect locally extended chain segments. Smaller amplitude RDCs in the N-terminal region occur largely in regions of positive shift deviations, although the RDCs do not change sign as would be expected for more highly populated helical structure. Adapted from [26].
Figure 2
Figure 2. NMR PRE in α-, β- and γ-synuclein
A paramagnetic spin label attached to a cysteine introduced at position 20 leads to clear broadening in the C-terminal tail of α-synuclein, but not of β- or γ-synuclein, suggesting long-range N- to C-terminal contacts are present in the former but not in the latter. The red lines represent the predicted broadening for an idealized random coil. Adapted from [26].
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References

    1. Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol. 2004;337:635–645. - PubMed
    1. Oldfield CJ, Cheng Y, Cortese MS, Brown CJ, Uversky VN, Dunker AK. Comparing and combining predictors of mostly disordered proteins. Biochemistry. 2005;44:1989–2000. - PubMed
    1. Tompa P, Dosztanyi Z, Simon I. Prevalent structural disorder in E. coli and S. cerevisiae proteomes. J Proteome Res. 2006;5:1996–2000. - PubMed
    1. Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol. 2005;6:197–208. - PubMed
    1. Fink AL. Natively unfolded proteins. Curr Opin Struct Biol. 2005;15:35–41. - PubMed

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