Evidence map›Paper›PMID 19876372›Full record

ArticlePLoS computational biology2009

Mechanical strength of 17,134 model proteins and cysteine slipknots.

Mateusz Sikora, Joanna I Sułkowska, Marek Cieplak

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 114 citations in OpenAlex.

  1. ProtAgents: protein discoveryDigital discovery · 2024
    Article
  2. MechanoProDB: a web-based database for exploring the mechanical properties of proteins.Database : the journal of biological databases and curation · 2024
    Article
  3. Article
  4. Review
  5. Article
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  8. Article
  9. Nascent Folding of Proteins Across the Three Domains of Life.Frontiers in molecular biosciences · 2021
    Article
  10. Article
  11. Article
  12. Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins.Journal of chemical theory and computation · 2020
    Article
  13. Article
  14. Self-assembly of model proteins into virus capsids.Journal of physics. Condensed matter : an Institute of Physics journal · 2017
    Article
  15. Review
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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

3 authors at 2 institutions in 2 countries.

Mateusz SikoraInstitute of Physics, Polish Academy of Sciences, Warsaw, Poland.
Joanna I Sułkowska
Marek Cieplak
Institute of Physics · PLPolish Academy of Sciences · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A new theoretical survey of proteins' resistance to constant speed stretching is performed for a set of 17,134 proteins as described by a structure-based model. The proteins selected have no gaps in their structure determination and consist of no more than 250 amino acids. Our previous studies have dealt with 7510 proteins of no more than 150 amino acids. The proteins are ranked according to the strength of the resistance. Most of the predicted top-strength proteins have not yet been studied experimentally. Architectures and folds which are likely to yield large forces are identified. New types of potent force clamps are discovered. They involve disulphide bridges and, in particular, cysteine slipknots. An effective energy parameter of the model is estimated by comparing the theoretical data on characteristic forces to the corresponding experimental values combined with an extrapolation of the theoretical data to the experimental pulling speeds. These studies provide guidance for future experiments on single molecule manipulation and should lead to selection of proteins for applications. A new class of proteins, involving cysteine slipknots, is identified as one that is expected to lead to the strongest force clamps known. This class is characterized through molecular dynamics simulations.

Indexed as

Models, MolecularMolecular Dynamics SimulationAmino AcidsCysteineElasticityHumansProtein FoldingProteinsTensile StrengthAmino AcidsCysteineProteins

Identifiers

PMID19876372
PMCPMC2759523
OpenAlexW2015191244

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.