Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy

In order to understand the conformational behaviour of Intrinsically Disordered Proteins (IDPs), it is essential to develop a molecular representation of the partially folded state. Due to the very large number of degrees of conformational freedom available to such a disordered system, this problem...

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Bibliographic Details
Published in:Molecular bioSystems 2012-01, Vol.8 (1), p.58-68
Main Authors: Schneider, Robert, Huang, Jie-rong, Yao, Mingxi, Communie, Guillaume, Ozenne, Valéry, Mollica, Luca, Salmon, Loïc, Jensen, Malene Ringkjøbing, Blackledge, Martin
Format: Article
Language:English
Subjects:
Animals
Humans
Magnetic Resonance Spectroscopy - methods
Protein Conformation
Protein Folding
Proteins - chemistry
Proteins - metabolism
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Summary:In order to understand the conformational behaviour of Intrinsically Disordered Proteins (IDPs), it is essential to develop a molecular representation of the partially folded state. Due to the very large number of degrees of conformational freedom available to such a disordered system, this problem is highly underdetermined. Characterisation therefore requires extensive experimental data, and novel analytical tools are required to exploit the specific conformational sensitivity of different experimental parameters. In this review we concentrate on the use of nuclear magnetic resonance (NMR) spectroscopy for the study of conformational behaviour of IDPs at atomic resolution. Each experimental NMR parameter is sensitive to different aspects of the structural and dynamic behaviour of the disordered state and requires specific consideration of the relevant averaging properties of the physical interaction. In this review we present recent advances in the description of disordered proteins and the selection of representative ensembles on the basis of experimental data using statistical coil sampling from flexible-meccano and ensemble selection using ASTEROIDS. Using these tools we aim to develop a unified molecular representation of the disordered state, combining complementary data sets to extract a meaningful description of the conformational behaviour of the protein.
ISSN:1742-206X
1742-2051
DOI:10.1039/c1mb05291h