Evidence map›Paper›PMID 25739366›Full record

ArticleProteins2015

On the relationship between NMR-derived amide order parameters and protein backbone entropy changes.

Kim A Sharp, Evan O'Brien, Vignesh Kasinath, A Joshua Wand

Abstract read
In one paragraph

Article in Proteins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Intrinsic conformational equilibria position arrestin-2 for activation.Protein science : a publication of the Protein Society · 2026
    Article
  2. Intrinsic conformational equilibria position arrestin-2 for activation.bioRxiv : the preprint server for biology · 2025
    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

4 authors.

Kim A SharpGraduate Group in Biochemistry and Molecular Biophysics and the Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, 19104.
Evan O'Brien
Vignesh Kasinath
A Joshua Wand

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Innovative Supercomputing for Breakthrough Molecular DynamicsRC2GM093307 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI DITTRICH, MARKUS · 2009 to 2010
$2.7M
Fluctuations and entropy in the energetics and function of protein complexesR01GM102447 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 2012 to 2015
$1.4M
NIGMS NIH HHS GM102447NIGMS NIH HHS R01 GM102447NIGMS NIH HHS RC2 GM093307NIGMS NIH HHS RC2GM093307NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

Molecular dynamics simulations are used to analyze the relationship between NMR-derived squared generalized order parameters of amide NH groups and backbone entropy. Amide order parameters (O(2) NH ) are largely determined by the secondary structure and average values appear unrelated to the overall flexibility of the protein. However, analysis of the more flexible subset (O(2) NH  < 0.8) shows that these report both on the local flexibility of the protein and on a different component of the conformational entropy than that reported by the side chain methyl axis order parameters, O(2) axis . A calibration curve for backbone entropy vs. O(2) NH is developed, which accounts for both correlations between amide group motions of different residues, and correlations between backbone and side chain motions. This calibration curve can be used with experimental values of O(2) NH changes obtained by NMR relaxation measurements to extract backbone entropy changes, for example, upon ligand binding. In conjunction with our previous calibration for side chain entropy derived from measured O(2) axis values this provides a prescription for determination of the total protein conformational entropy changes from NMR relaxation measurements.

Indexed as

AmidesEntropyHydrogen BondingMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProteinsProtein Structure, SecondaryAmidesProteinsbackbone motionconformational entropymolecular dynamicsNMR relaxationprotein motion

Identifiers

PMID25739366
PMCPMC4400257

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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.