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Atomic-level characterization of disordered protein ensembles

Mittag, Tanja, Forman-Kay, Julie D·2007·Current Opinion in Structural Biology
DOI 10.1016/j.sbi.2007.01.009
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Abstract

The roles of unfolded states of proteins in normal folding and in diseases involving aggregation, as well as the prevalence and regulatory functions of intrinsically disordered proteins, have become increasingly recognized. The structural representation of these disordered states as ensembles of interconverting conformers can therefore provide critical insights. Experimental methods can be used to probe ensemble-averaged structural properties of disordered states and computational approaches generate representative ensembles of conformers using experimental restraints. In particular, NMR and small-angle X-ray scattering provide quantitative data that can readily be incorporated into calculations. These techniques have gleaned structural information about denatured, unfolded and intrinsically disordered proteins. The use of experimental data in different computational approaches, including ensemble molecular dynamics simulations and algorithms that assign populations to pregenerated conformers, has highlighted the presence of both local and long-range structure, and the occurrence of native-like and non-native interactions in unfolded and denatured states. Analysis of the resulting ensembles has suggested important implications of this fluctuating structure for folding, aggregation and binding.

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Metadata

Authors
Mittag, T., & Forman-Kay, J. D.
Venue
Current Opinion in Structural Biology
Publisher
Elsevier BV
Published
2007-02
Volume
17
Issue
1
Pages
3-14
ISSN
0959-440X
DOI
10.1016/j.sbi.2007.01.009
Cited by
423
References
2
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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