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Volume 169, 2014
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Visualising intrinsic disorder and conformational variation in protein ensembles

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Abstract

Intrinsically disordered regions (IDRs) in proteins are still not well understood, but are increasingly recognised as important in key biological functions, as well as in diseases. IDRs often confound experimental structure determination—however, they are present in many of the available 3D structures, where they exhibit a wide range of conformations, from ill-defined and highly flexible to well-defined upon binding to partner molecules, or upon post-translational modifications. Analysing such large conformational variations across ensembles of 3D structures can be complex and difficult; our goal in this paper is to improve this situation by augmenting traditional approaches (molecular graphics and principal components) with methods from human–computer interaction and information visualisation, especially parallel coordinates. We present a new tool integrating these approaches, and demonstrate how it can dissect ensembles to reveal functional insights into conformational variation and intrinsic disorder.

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Article information


Submitted
14 Dec 2013
Accepted
20 Feb 2014
First published
21 Feb 2014

Faraday Discuss., 2014,169, 179-193
Article type
Paper
Author version available

Visualising intrinsic disorder and conformational variation in protein ensembles

J. Heinrich, M. Krone, S. I. O'Donoghue and D. Weiskopf, Faraday Discuss., 2014, 169, 179
DOI: 10.1039/C3FD00138E

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