Evidence map›Paper›PMID 27358108›Full record

ArticleScientific reports2016

A Structure-free Method for Quantifying Conformational Flexibility in proteins.

Virginia M Burger, Daniel J Arenas, Collin M Stultz

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed.

  1. Article
  2. Structural and Mechanical Dynamics of Polymer Membranes Across Multilength Scales.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Journal of the American Chemical Society · 2026
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  17. Getting Smaller by Denaturation: Acid-Induced Compaction of Antibodies.The journal of physical chemistry letters · 2023
    Article
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Virginia M BurgerResearch Laboratory for Electronics, Massachusetts Institute of Technology, 77 Massachusetts Ave. Cambridge MA 02139, USA.
Daniel J ArenasDepartment of Physics, University of North Florida, 1 University of North Fl Dr, Jacksonville, FL 32224, USA.
Collin M StultzResearch Laboratory for Electronics, Massachusetts Institute of Technology, 77 Massachusetts Ave. Cambridge MA 02139, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

All proteins sample a range of conformations at physiologic temperatures and this inherent flexibility enables them to carry out their prescribed functions. A comprehensive understanding of protein function therefore entails a characterization of protein flexibility. Here we describe a novel approach for quantifying a protein's flexibility in solution using small-angle X-ray scattering (SAXS) data. The method calculates an effective entropy that quantifies the diversity of radii of gyration that a protein can adopt in solution and does not require the explicit generation of structural ensembles to garner insights into protein flexibility. Application of this structure-free approach to over 200 experimental datasets demonstrates that the methodology can quantify a protein's disorder as well as the effects of ligand binding on protein flexibility. Such quantitative descriptions of protein flexibility form the basis of a rigorous taxonomy for the description and classification of protein structure.

Indexed as

Models, ChemicalProtein ConformationAlgorithmsBacterial ProteinsDatasets as TopicModels, MolecularMolecular Dynamics SimulationScattering, Small AngleSolutionsThermodynamicsX-Ray DiffractionBacterial ProteinsCcdA protein, BacteriaCcdB protein, Plasmid FSolutions

Identifiers

PMID27358108
PMCPMC4928179

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.