Evidence map›Paper›PMID 30668901›Full record

ArticleAnalytical chemistry2019

Versatile Analysis of DNA-Biomolecule Interactions in Solution by Hydrodynamic Separation and Single Molecule Detection.

Sarah M Friedrich, Rachel Bang, Andrew Li, Tza-Huei Wang

Abstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Messenger RNA and guide RNA distributions in lipid nanoparticles impact gene-editing efficiency in vivo.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
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.

Sarah M FriedrichORCID 0000-0001-9954-5438
Rachel Bang
Andrew Li
Tza-Huei Wang

Funding

BIOMEDICAL ENGINEERING TRAINING PROGRAMT32GM007057 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI KANOLD, PATRICK O, KARCHIN, RACHEL · 1985 to 2023
$10.4M
A Droplet-based single cell platform for pathogen identification and ASTR01AI117032 · NIAID · JOHNS HOPKINS UNIVERSITY · PI LIAO, JOSEPH C, WANG, TZA-HUEI JEFF · 2015 to 2019
$5.7M
A "Culture" Shift: Integrated Bacterial Screening and Antibacterial Susceptibility Test on Microfluidic Digital Array for Bloodstream InfectionsR01AI137272 · NIAID · JOHNS HOPKINS UNIVERSITY · PI WANG, TZA-HUEI JEFF, YANG, SAMUEL · 2018 to 2022
$3.6M
PicoSep - A Microfluidic Platform for Single Molecule DNA and RNA SizingR44GM103356 · NIGMS · CIRCULOMICS, INC. · PI LIU, KELVIN, WANG, TZA-HUEI JEFF · 2017 to 2018
$1.5M
Digital Detection of Tumor-Derived Circulating Methylated DNAR21CA186809 · NCI · JOHNS HOPKINS UNIVERSITY · PI WANG, TZA-HUEI JEFF · 2014 to 2016
$698k
Acquisition of GE Typhoon FLA9500 Variable Mode ImagerS10OD021567 · OD · JOHNS HOPKINS UNIVERSITY · PI MCCAFFERY, J. MICHAEL · 2017 to 2017
$147k
NCI NIH HHS R21 CA186809NIAID NIH HHS R01 AI117032NIAID NIH HHS R01 AI137272NIGMS NIH HHS R44 GM103356NIGMS NIH HHS T32 GM007057NIH HHS S10 OD021567
6 · The paper itself

Abstract

DNA can interact with a wide array of molecules with a range of binding affinities, stoichiometry, and size-scales. We present a sensitive, quantitative, and versatile platform for sensing and evaluating these diverse DNA-biomolecule interactions and DNA conformational changes in free solution. Single molecule free solution hydrodynamic separation utilizes differences in hydrodynamic mobility to separate bound DNA-biomolecule complexes from unbound DNA and determine the associated size change that results from binding. Single molecule detection enables highly quantitative analysis of the fraction of DNA in the bound and unbound state to characterize binding behavior including affinity, stoichiometry, and cooperativity. A stacked injection scheme increases throughput to enable practical analysis of DNA-biomolecule interactions using only picoliters of sample per measurement. To demonstrate analysis of DNA-protein interactions on a local scale, we investigate binding of the E. coli single stranded binding protein to two DNA oligos both individually and in direct competition. We show that stoichiometry and cooperativity is a function of DNA length and verify these differences in binding characteristics through direct competition. To demonstrate analysis of DNA-small molecule interactions and global conformational changes, we also assess DNA condensation with the polyamine spermidine. We use hydrodynamic mobility to evaluate the size of spermidine-condensed DNA and single molecule burst analysis to evaluate DNA packing within the condensed globules relative to free-coiled DNA. This platform thus presents a versatile tool capable of quantitative and sensitive evaluation of diverse biomolecular interactions, complex properties, and binding characteristics.

Indexed as

Binding SitesDNADNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsHydrodynamicsNucleic Acid ConformationProtein BindingSingle Molecule ImagingDNADNA-Binding ProteinsEscherichia coli ProteinsSSB protein, E coli

Identifiers

PMID30668901
PMCPMC8648464

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Registered trials

None linked

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.