Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins

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Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins. / Thomasen, F. Emil; Lindorff-Larsen, Kresten.

In: Biochemical Society Transactions, Vol. 50, No. 1, 2022, p. 541-554.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Thomasen, FE & Lindorff-Larsen, K 2022, 'Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins', Biochemical Society Transactions, vol. 50, no. 1, pp. 541-554. https://doi.org/10.1042/BST20210499

APA

Thomasen, F. E., & Lindorff-Larsen, K. (2022). Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins. Biochemical Society Transactions, 50(1), 541-554. https://doi.org/10.1042/BST20210499

Vancouver

Thomasen FE, Lindorff-Larsen K. Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins. Biochemical Society Transactions. 2022;50(1):541-554. https://doi.org/10.1042/BST20210499

Author

Thomasen, F. Emil ; Lindorff-Larsen, Kresten. / Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins. In: Biochemical Society Transactions. 2022 ; Vol. 50, No. 1. pp. 541-554.

Bibtex

@article{62891b71a5ce418aa2ea1f8836f8e682,
title = "Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins",
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. ",
author = "Thomasen, {F. Emil} and Kresten Lindorff-Larsen",
note = "Publisher Copyright: {\textcopyright} 2022 The Author(s).",
year = "2022",
doi = "10.1042/BST20210499",
language = "English",
volume = "50",
pages = "541--554",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins

AU - Thomasen, F. Emil

AU - Lindorff-Larsen, Kresten

N1 - Publisher Copyright: © 2022 The Author(s).

PY - 2022

Y1 - 2022

N2 - 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.

AB - 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.

U2 - 10.1042/BST20210499

DO - 10.1042/BST20210499

M3 - Review

C2 - 35129612

AN - SCOPUS:85125554475

VL - 50

SP - 541

EP - 554

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 1

ER -

ID: 302900280