Pith. Sign in

RECORD

Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins

PaperPDF from arXiv

data files

Paper breakdownThe authors' claims, conditions and measurements, as JSON Signed receiptProof this review has not been altered
X Bluesky LinkedIn Reddit Hacker News
F. Emil Thomasen, Kresten Lindorff-Larsen

Biomolecules · Submitted 10 Dec 2021

abstract compiled · 2026-09-23 · no language-model review

The authors' main claim 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.

how it is stated · asserted 1.00 read the record →

Comment (0) Read on arXiv ↗
Cite ▾
arXiv ID2112.05527 (version 1)
Pith ID32JG7H7E, Pith's permanent record of this paper and its review
CitationF. Emil Thomasen, Kresten Lindorff-Larsen. "Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins." arXiv:2112.05527 (2021). https://pith.science/paper/32JG7H7E
Claim paper

The compiled record

The paper's own sentences, arranged. Each label is drawn from a closed vocabulary; the number beside it is the probability the classifier gave that label. Numbers in the tables are the authors', checked by code. No sentence in this record was written by a model.

Open the compiled record

Compiled by classifier-1.13.0 via TypeSafe API, question bank abstract-p1-20260923, 2026-09-23: 1 request, 3,768 input tokens.

What the abstract itself states, as probabilities: claims first 0.02 · states limitation 0.05 · human participants 0.03 · controlled comparison 0.02 · randomized assignment 0.01 · states quantitative result 0.03 · compares with prior results 0.05 · mentions code or data availability 0.02.

The abstract, sentence by sentence

arXiv listing abstract v1. Results and the main claim are underlined; .

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 integration of biophysical experiments and computational models. In this review, we discuss current approaches to determining 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.

background contribution method result interpretation main claim

What the classifier reports for each sentence. The number is the probability it gave the label.
#sentencerolethe authors' own workstates the main conclusionstrength
s0 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. background 1.00 0.06 0.23 asserted 1.00
s1 Determining conformational ensembles usually involves integration of biophysical experiments and computational models. background 0.94 0.05 0.05 asserted 0.99
s2 In this review, we discuss current approaches to determining 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. contribution 0.97 0.17 0.13 asserted 0.89
s3 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. future work 0.72 0.46 0.11 asserted 0.78

What kind of paper the classifier reports this is: review 1.00 · evidence from literature 1.00.

What was examined, and what was not

sources read
  • arXiv listing abstract v1
not examined
  • full text
  • figures and tables
  • references and citing sentences
  • relations to other papers
levels run
  • P abstract
not run
  • S sections
  • T body sentences
  • C citations
  • R cross-paper relations

Every quoted sentence on this record is the authors'. Every label is from Pith's closed vocabulary, with the probability shown beside it. Every number in the measurements table is the authors', checked by code. Record as JSON

The paper
Original 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 integration of biophysical experiments and computational models. In this review, we discuss current approaches to determining 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.

Human review

How Pith checks papers → · Full audit of this paper →

Discussion

Know something about this paper? Leave a comment, or highlight any passage above to comment on it.