Evidence map›Paper›PMID 27573845›Full record

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

Synthetic beta-solenoid proteins with the fragment-free computational design of a beta-hairpin extension.

James T MacDonald, Burak V Kabasakal, David Godding, Sebastian Kraatz, Louie Henderson, James Barber, Paul S Freemont, James W Murray

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
2.8field-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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. A peripheral carboxysome component regulates cyanobacterial glycogen deposition.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  3. Novel Knotted Solenoid fold with order-shifted coil arrangement leads to nontrivial 3Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Parametrically guided design of beta barrels and transmembrane nanopores using deep learning.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  7. Article
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  9. Article
  10. Review
  11. Article
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  14. Review
  15. The ascent of man(made oxidoreductases).Current opinion in structural biology · 2018
    Review
  16. Folding cooperativity and allosteric function in the tandem-repeat protein class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  17. CCBuilder 2.0: Powerful and accessible coiled-coil modeling.Protein science : a publication of the Protein Society · 2018
    Article
  18. Article
  19. Review
  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

8 authors at 1 institution in 2 countries.

James T MacDonaldCentre for Synthetic Biology and Innovation, Imperial College London, London SW7 2AZ, United Kingdom; Department of Medicine, Imperial College London, London SW7 2AZ, United Kingdom;
Burak V KabasakalDepartment of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom;
David GoddingDepartment of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom; Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom;
Sebastian KraatzDepartment of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom; Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland.
Louie HendersonDepartment of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom;
James BarberDepartment of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom;
Paul S FreemontCentre for Synthetic Biology and Innovation, Imperial College London, London SW7 2AZ, United Kingdom; Department of Medicine, Imperial College London, London SW7 2AZ, United Kingdom;
James W MurrayDepartment of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom; j.w.murray@imperial.ac.uk.
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F023308/1
6 · The paper itself

Abstract

The ability to design and construct structures with atomic level precision is one of the key goals of nanotechnology. Proteins offer an attractive target for atomic design because they can be synthesized chemically or biologically and can self-assemble. However, the generalized protein folding and design problem is unsolved. One approach to simplifying the problem is to use a repetitive protein as a scaffold. Repeat proteins are intrinsically modular, and their folding and structures are better understood than large globular domains. Here, we have developed a class of synthetic repeat proteins based on the pentapeptide repeat family of beta-solenoid proteins. We have constructed length variants of the basic scaffold and computationally designed de novo loops projecting from the scaffold core. The experimentally solved 3.56-Å resolution crystal structure of one designed loop matches closely the designed hairpin structure, showing the computational design of a backbone extension onto a synthetic protein core without the use of backbone fragments from known structures. Two other loop designs were not clearly resolved in the crystal structures, and one loop appeared to be in an incorrect conformation. We have also shown that the repeat unit can accommodate whole-domain insertions by inserting a domain into one of the designed loops.

Indexed as

Protein ConformationAmino Acid SequenceCrystallography, X-RayPeptidesProtein EngineeringProtein FoldingProteinsProtein Structure, SecondaryRepetitive Sequences, Amino AcidPeptidesProteinscoarse-grained modelcomputational protein designde novo backbone designsynthetic repeat proteins

Identifiers

PMID27573845
PMCPMC5027453
OpenAlexW2517037156

What OpenQuestion holds

Textmetadata
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.