Evidence map›Paper›PMID 22272723›Full record

ArticleThe journal of physical chemistry. B2012

Further evidence for the likely completeness of the library of solved single domain protein structures.

Jeffrey Skolnick, Hongyi Zhou, Michal Brylinski

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Multistep mutational transformation of a protein fold through structural intermediates.Protein science : a publication of the Protein Society · 2018
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Biophysics of protein evolution and evolutionary protein biophysics.Journal of the Royal Society, Interface · 2014
    Article
  13. Article
  14. Template-based structure modeling of protein-protein interactions.Current opinion in structural biology · 2014
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Interplay of physics and evolution in the likely origin of protein biochemical function.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

3 authors.

Jeffrey SkolnickCenter for the Study of Systems Biology, Georgia Institute of Technology, 250 14th Street NW, Atlanta, Georgia 30318, USA. skolnick@gatech.edu
Hongyi Zhou
Michal Brylinski

Funding

Interaction Pattern Based Predictor of Protein StruturesR01GM048835 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SKOLNICK, JEFFREY · 1994 to 2015
$4.0M
THEORY OF FOLDING TRANSITIONS IN A-HELICAL PROTEINSR01GM037408 · NIGMS · WASHINGTON UNIVERSITY · PI SKOLNICK, JEFFREY · 1987 to 2014
$3.9M
NIGMS NIH HHS GM-48835NIGMS NIH HHS R01 GM037408NIGMS NIH HHS R01 GM048835
6 · The paper itself

Abstract

Recent studies questioned whether the Protein Data Bank (PDB) contains all compact, single domain protein structures. Here, we show that all quasi-spherical, QS, random protein structures devoid of secondary structure are in the PDB and are excellent templates for all native PDB proteins up to 250 residues. Because QS templates have a similar global contour as native, TASSER can refine 98% (90%) of those whose TM-score is 0.4 (0.35) to structures greater than or equal to the 0.5 TM-score threshold (0.74 (0.64) mean TM-score) for CATH/SCOP assignment. On the basis of this and the fact that, at a TM-score of 0.4, 83% (90%) of all (internal) core secondary structure elements are recovered, a 0.40 TM-score is an appropriate fold similarity assignment threshold. Despite the claims of Taylor, Trovato, and Zhou that many of their structures lack a PDB counterpart, using fr-TM-align, at a 0.45 (0.5) TM-score threshold, essentially all (most) are found in the PDB. Thus, the conclusion that the PDB is likely complete is further supported.

Indexed as

AlgorithmsDatabases, ProteinModels, MolecularPeptide LibraryProteinsProtein Structure, SecondaryPeptide LibraryProteins

Identifiers

PMID22272723
PMCPMC3351587

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.