Evidence map›Paper›PMID 28470607›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2017

Protein Folding Using a Vortex Fluidic Device.

Joshua Britton, Joshua N Smith, Colin L Raston, Gregory A Weiss

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Under-5-Minute Immunoblot Assays by Vortex Fluidic Device Acceleration.Angewandte Chemie (International ed. in English) · 2022
    Article
  2. 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.

Joshua BrittonDepartment of Chemistry, University of California, Irvine, 1102 Natural Sciences 2, Irvine, CA, 92697-2025, USA.
Joshua N SmithDepartment of Molecular Biology and Biochemistry, University of California, Irvine, 1102 Natural Sciences 2, Irvine, CA, 92697-2025, USA.
Colin L RastonCentre for NanoScale Science and Technology, School of Chemical and Physical Sciences, Flinders University, Adelaide, SA, 5001, Australia. colin.raston@flinders.edu.au.
Gregory A WeissDepartment of Chemistry, University of California, Irvine, 1102 Natural Sciences 2, Irvine, CA, 92697-2025, USA. gweiss@uci.edu.

Funding

Membrane Protein Co- Crystallization with Highly Crystalline and Soluble ProteinsR01GM100700 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WEISS, GREGORY A. · 2012 to 2015
$1.1M
NIGMS NIH HHS R01 GM100700
6 · The paper itself

Abstract

Essentially all biochemistry and most molecular biology experiments require recombinant proteins. However, large, hydrophobic proteins typically aggregate into insoluble and misfolded species, and are directed into inclusion bodies. Current techniques to fold proteins recovered from inclusion bodies rely on denaturation followed by dialysis or rapid dilution. Such approaches can be time consuming, wasteful, and inefficient. Here, we describe rapid protein folding using a vortex fluidic device (VFD). This process uses mechanical energy introduced into thin films to rapidly and efficiently fold proteins. With the VFD in continuous flow mode, large volumes of protein solution can be processed per day with 100-fold reductions in both folding times and buffer volumes.

Indexed as

HydrodynamicsProtein FoldingAnimalsBuffersChickensEquipment DesignEscherichia coliGene ExpressionMuramidasePhysicsProtein DenaturationRecombinant ProteinsUp-RegulationBuffershen egg lysozymeMuramidaseRecombinant ProteinsBacterial protein expressionContinuous flowInclusion bodiesMisfolded proteinsProtein foldingVortex fluidics

Identifiers

PMID28470607
PMCPMC5999337

What OpenQuestion holds

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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.