Evidence map›Paper›PMID 25004800›Full record

ArticleScientific reports2014

Differential Scanning Fluorimetry provides high throughput data on silk protein transitions.

Fritz Vollrath, Nick Hawkins, David Porter, Chris Holland, Maxime Boulet-Audet

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 9% of its field
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

17 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Microcompartmentalization Controls Silk Feedstock Rheology.Langmuir : the ACS journal of surfaces and colloids · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Guided inquiry activity linking thermodynamic parameters of protein unfolding to structure using differential scanning fluorimetry data in the biophysical chemistry classroom.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

Fritz VollrathDepartment of Zoology, University of Oxford, South Parks Rd, Oxford OX1 3PS.
Nick HawkinsDepartment of Zoology, University of Oxford, South Parks Rd, Oxford OX1 3PS.
David PorterDepartment of Zoology, University of Oxford, South Parks Rd, Oxford OX1 3PS.
Chris Holland1] Department of Zoology, University of Oxford, South Parks Rd, Oxford OX1 3PS [2] Department of Materials Science and Engineering, University of Sheffield, Mappin Street, Sheffield, S1 3JD, UK.
Maxime Boulet-Audet1] Department of Zoology, University of Oxford, South Parks Rd, Oxford OX1 3PS [2] Department of Chemical Engineering and Department of Life Sciences, Imperial College London, South Kensington Campus, London.
University of Oxford · GBImperial College London · GB

Funding

European Research Council 233409
6 · The paper itself

Abstract

Here we present a set of measurements using Differential Scanning Fluorimetry (DSF) as an inexpensive, high throughput screening method to investigate the folding of silk protein molecules as they abandon their first native melt conformation, dehydrate and denature into their final solid filament conformation. Our first data and analyses comparing silks from spiders, mulberry and wild silkworms as well as reconstituted 'silk' fibroin show that DSF can provide valuable insights into details of silk denaturation processes that might be active during spinning. We conclude that this technique and technology offers a powerful and novel tool to analyse silk protein transitions in detail by allowing many changes to the silk solutions to be tested rapidly with microliter scale sample sizes. Such transition mechanisms will lead to important generic insights into the folding patterns not only of silks but also of other fibrous protein (bio)polymers.

Indexed as

AnimalsBombyxFibroinsFluorometryMorusProtein FoldingSilkSpidersFibroinsSilk

Identifiers

PMID25004800
PMCPMC4088128
OpenAlexW1990966214

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

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.