Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10883562 | Progress in Biophysics and Molecular Biology | 2015 | 6 Pages |
Abstract
Intrinsically disordered proteins are increasingly the focus of biological research since their significance was acknowledged over a decade ago. Due to their importance in biomolecular interactions, they are found to play key roles in many diseases such as cancers and amyloidoses. However, because they lack stable structure they pose a challenge for many experimental methods that are traditionally used to study proteins. Atomistic molecular dynamics simulations can help get around many of the problems faced by such methods provided appropriate timescales are sampled and underlying empirical force fields are applicable. This review presents recent works that highlight the power and potential of atomistic simulations to transform the investigatory pipeline by providing critical insights into the behavior and interactions of intrinsically disordered proteins.
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Authors
Nathaniel Stanley, Santiago Esteban-MartÃn, Gianni De Fabritiis,