Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins

F. Emil Thomasen, Kresten Lindorff-Larsen*

*Corresponding author af dette arbejde

Publikation: Bidrag til tidsskriftReviewForskningpeer review

39 Citationer (Scopus)
7 Downloads (Pure)

Abstract

Intrinsically disordered proteins (IDPs) and multidomain proteins with flexible linkers show a high level of structural heterogeneity and are best described by ensembles consisting of multiple conformations with associated thermodynamic weights. Determining conformational ensembles usually involves the integration of biophysical experiments and computational models. In this review, we discuss current approaches to determine conformational ensembles of IDPs and multidomain proteins, including the choice of biophysical experiments, computational models used to sample protein conformations, models to calculate experimental observables from protein structure, and methods to refine ensembles against experimental data. We also provide examples of recent applications of integrative conformational ensemble determination to study IDPs and multidomain proteins and suggest future directions for research in the field.

OriginalsprogEngelsk
TidsskriftBiochemical Society Transactions
Vol/bind50
Udgave nummer1
Sider (fra-til)541-554
Antal sider14
ISSN0300-5127
DOI
StatusUdgivet - 2022

Bibliografisk note

Funding Information:
Our work in this area is supported by the Lundbeck Foundation BRAINSTRUC initiative (R155-2015-2666 to K. L.-L.).

Publisher Copyright:
© 2022 The Author(s).

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