Evidence map›Paper›PMID 35902573›Full record

ArticleNature communications2022

Protein secondary structure in spider silk nanofibrils.

Qijue Wang, Patrick McArdle, Stephanie L Wang, Ryan L Wilmington, Zhen Xing, Alexander Greenwood, Myriam L Cotten, M Mumtaz Qazilbash, Hannes C Schniepp

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

22 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Manipulating the Assembly and Architecture of Fibrillar Silk.Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  7. Article
  8. Elasticity Anisotropy ofBiomacromolecules · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Structural analysis of silk using solid-state NMR.Magnetic resonance letters · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

9 authors at 1 institution in 1 country.

Qijue WangDepartment of Applied Science, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA.ORCID 0000-0002-7364-155X
Patrick McArdleDepartment of Physics, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA.
Stephanie L WangDepartment of Physics, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA.
Ryan L WilmingtonDepartment of Physics, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA.ORCID 0000-0001-5787-3281
Zhen XingDepartment of Physics, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA.ORCID 0000-0002-6444-4204
Alexander GreenwoodDepartment of Applied Science, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA.
Myriam L CottenDepartment of Applied Science, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA.
M Mumtaz QazilbashDepartment of Physics, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA.
Hannes C SchnieppDepartment of Applied Science, William & Mary, P.O. Box 8795, Williamsburg, VA, 23187-8795, USA. schniepp@wm.edu.ORCID 0000-0003-4645-9469
William & Mary · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nanofibrils play a pivotal role in spider silk and are responsible for many of the impressive properties of this unique natural material. However, little is known about the internal structure of these protein fibrils. We carry out polarized Raman and polarized Fourier-transform infrared spectroscopies on native spider silk nanofibrils and determine the concentrations of six distinct protein secondary structures, including β-sheets, and two types of helical structures, for which we also determine orientation distributions. Our advancements in peak assignments are in full agreement with the published silk vibrational spectroscopy literature. We further corroborate our findings with X-ray diffraction and magic-angle spinning nuclear magnetic resonance experiments. Based on the latter and on polypeptide Raman spectra, we assess the role of key amino acids in different secondary structures. For the recluse spider we develop a highly detailed structural model, featuring seven levels of structural hierarchy. The approaches we develop are directly applicable to other proteinaceous materials.

Indexed as

SilkSpidersAnimalsMagnetic Resonance SpectroscopyProtein Structure, SecondarySpectroscopy, Fourier Transform InfraredX-Ray DiffractionSilk

Identifiers

PMID35902573
PMCPMC9334623
OpenAlexW4288436665

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.