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Review

Intrinsically Disordered Proteins: Where Computation Meets Experiment

1
Research Laboratory of Electronics, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA
2
Computational and Systems Biology Initiative, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA
3
Department of Electrical Engineering and Computer Science, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA
4
Institute for Medical Engineering and Science, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA
*
Author to whom correspondence should be addressed.
Polymers 2014, 6(10), 2684-2719; https://doi.org/10.3390/polym6102684
Received: 28 August 2014 / Revised: 10 October 2014 / Accepted: 13 October 2014 / Published: 23 October 2014
(This article belongs to the Special Issue Computational Chemistry)
Proteins are heteropolymers that play important roles in virtually every biological reaction. While many proteins have well-defined three-dimensional structures that are inextricably coupled to their function, intrinsically disordered proteins (IDPs) do not have a well-defined structure, and it is this lack of structure that facilitates their function. As many IDPs are involved in essential cellular processes, various diseases have been linked to their malfunction, thereby making them important drug targets. In this review we discuss methods for studying IDPs and provide examples of how computational methods can improve our understanding of IDPs. We focus on two intensely studied IDPs that have been implicated in very different pathologic pathways. The first, p53, has been linked to over 50% of human cancers, and the second, Amyloid-β (Aβ), forms neurotoxic aggregates in the brains of patients with Alzheimer’s disease. We use these representative proteins to illustrate some of the challenges associated with studying IDPs and demonstrate how computational tools can be fruitfully applied to arrive at a more comprehensive understanding of these fascinating heteropolymers. View Full-Text
Keywords: intrinsically disordered proteins; molecular dynamics; p53; Amyloid-β (Aβ) intrinsically disordered proteins; molecular dynamics; p53; Amyloid-β (Aβ)
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MDPI and ACS Style

Burger, V.M.; Gurry, T.; Stultz, C.M. Intrinsically Disordered Proteins: Where Computation Meets Experiment. Polymers 2014, 6, 2684-2719. https://doi.org/10.3390/polym6102684

AMA Style

Burger VM, Gurry T, Stultz CM. Intrinsically Disordered Proteins: Where Computation Meets Experiment. Polymers. 2014; 6(10):2684-2719. https://doi.org/10.3390/polym6102684

Chicago/Turabian Style

Burger, Virginia M., Thomas Gurry, and Collin M. Stultz 2014. "Intrinsically Disordered Proteins: Where Computation Meets Experiment" Polymers 6, no. 10: 2684-2719. https://doi.org/10.3390/polym6102684

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