Evidence map›Paper›PMID 26960999›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Origin and prediction of free-solution interaction studies performed label-free.

Darryl J Bornhop, Michael N Kammer, Amanda Kussrow, Robert A Flowers, Jens Meiler

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
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  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Integrated Biomarkers for the Management of Indeterminate Pulmonary Nodules.American journal of respiratory and critical care medicine · 2021
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. An experimental check of backscattering interferometry.Sensors and actuators. B, Chemical · 2017
    Article
  18. Article
  19. Article
  20. Article does not explain the origin of free-solution protein interaction signals.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Darryl J BornhopDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235; The Vanderbilt Institute for Chemical Biology, Vanderbilt University, Nashville, TN 37235; darryl.bornhop@vanderbilt.edu.
Michael N KammerDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235; The Vanderbilt Institute for Chemical Biology, Vanderbilt University, Nashville, TN 37235; Department of Biomedical Engineering, Vanderbilt University, Nashville, TN 37235;
Amanda KussrowDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235; The Vanderbilt Institute for Chemical Biology, Vanderbilt University, Nashville, TN 37235;
Robert A FlowersDepartment of Chemistry, Lehigh University, Bethlehem, PA 18015;
Jens MeilerDepartment of Chemistry, Vanderbilt University, Nashville, TN 37235; The Vanderbilt Institute for Chemical Biology, Vanderbilt University, Nashville, TN 37235; Vanderbilt University Center for Structural Biology, Nashville, TN 37235.

Funding

Decrypting Variants of Uncertain Significance in Long-QT SyndromeR01HL122010 · NHLBI · VANDERBILT UNIVERSITY · PI GEORGE, ALFRED L., SANDERS, CHARLES R · 2014 to 2025
$15.5M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
ROSETTA An Integrated Protein Structure Modeling SuiteR01GM073151 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A · 2005 to 2019
$7.8M
Membrane Protein Structure Elucidation from sparse NMR data (KAMP)R01GM080403 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2007 to 2019
$3.0M
Computational Design of Protein-Ligand Interfaces - a Therapeutic StrategyR01GM099842 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2012 to 2015
$1.3M
Small Molecule Probes to Investigate Structure and Function of Y ReceptorsR01DK097376 · NIDDK · VANDERBILT UNIVERSITY · PI MEILER, JENS, WEAVER, C DAVID · 2013 to 2015
$1.0M
GPU-Accelerated Parallel Computer for Drug Discovery ApplicationsS10OD020154 · OD · VANDERBILT UNIVERSITY · PI SMITH, JARROD ANSON · 2015 to 2015
$225k
NHLBI NIH HHS R01 HL122010NIDDK NIH HHS R01 DK097376NIGMS NIH HHS P41 GM103311NIGMS NIH HHS P41-GM103311NIGMS NIH HHS R01 GM073151NIGMS NIH HHS R01 GM080403NIGMS NIH HHS R01 GM099842
6 · The paper itself

Abstract

Interaction/reaction assays have led to significant scientific discoveries in the biochemical, medical, and chemical disciplines. Several fundamental driving forces form the basis of intermolecular and intramolecular interactions in chemical and biochemical systems (London dispersion, hydrogen bonding, hydrophobic, and electrostatic), and in the past three decades the sophistication and power of techniques to interrogate these processes has developed at an unprecedented rate. In particular, label-free methods have flourished, such as NMR, mass spectrometry (MS), surface plasmon resonance (SPR), biolayer interferometry (BLI), and backscattering interferometry (BSI), which can facilitate assays without altering the participating components. The shortcoming of most refractive index (RI)-based label-free methods such as BLI and SPR is the requirement to tether one of the interaction entities to a sensor surface. This is not the case for BSI. Here, our hypothesis is that the signal origin for free-solution, label-free determinations can be attributed to conformation and hydration-induced changes in the solution RI. We propose a model for the free-solution response function (FreeSRF) and show that, when quality bound and unbound structural data are available, FreeSRF correlates well with the experiment (R(2)> 0.99, Spearman rank correlation coefficients >0.9) and the model is predictive within ∼15% of the experimental binding signal. It is also demonstrated that a simple mass-weighted dη/dC response function is the incorrect equation to determine that the change in RI is produced by binding or folding event in free solution.

Indexed as

Hydrogen BondingInterferometryModels, ChemicalProtein BindingProtein ConformationProtein FoldingRefractometrySensitivity and SpecificitySolutionsSolventsWaterSolutionsSolventsWaterassay methodologybackscattering interferometryconformation changehydration changemolecular interactions

Identifiers

PMID26960999
PMCPMC4812771

What OpenQuestion holds

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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.