Evidence map›Paper›PMID 22095563›Full record

ArticleProteins2012

Super folds, networks, and barriers.

Sean Burke, Ron Elber

Abstract read
In one paragraph

Article in Proteins, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Allelic diversity ofVeterinary and animal science · 2025
    Article
  2. Multistep mutational transformation of a protein fold through structural intermediates.Protein science : a publication of the Protein Society · 2018
    Article
  3. Article
  4. Article
  5. Comprehensive analysis of sequences of a protein switch.Protein science : a publication of the Protein Society · 2016
    Article
  6. Studying protein fold evolution with hybrids of differently folded homologs.Protein engineering, design & selection : PEDS · 2015
    Article
  7. Biophysics of protein evolution and evolutionary protein biophysics.Journal of the Royal Society, Interface · 2014
    Article
  8. A polymetamorphic protein.Protein science : a publication of the Protein Society · 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

2 authors.

Sean BurkeInstitute for Computational Engineering and Sciences, University of Texas at Austin, Austin, Texas 78712.
Ron Elber

Funding

LONG TIME DYNAMICS OF BIOMOLECULESR01GM059796 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ELBER, RON · 2000 to 2021
$5.7M
Optimization of Stuctures and Networks of ProteinsR01GM067823 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI ELBER, RON · 2004 to 2010
$1.9M
NIGMS NIH HHS GM067823NIGMS NIH HHS R01 GM059796NIGMS NIH HHS R01 GM067823
6 · The paper itself

Abstract

Exhaustive enumeration of sequences and folds is conducted for a simple lattice model of conformations, sequences, and energies. Examination of all foldable sequences and their nearest connected neighbors (sequences that differ by no more than a point mutation) illustrates the following: (i) There exist unusually large number of sequences that fold into a few structures (super-folds). The same observation was made experimentally and computationally using stochastic sampling and exhaustive enumeration of related models. (ii) There exist only a few large networks of connected sequences that are not restricted to one fold. These networks cover a significant fraction of fold spaces (super-networks). (iii) There exist barriers in sequence space that prevent foldable sequences of the same structure to "connect" through a series of single point mutations (super-barrier), even in the presence of the sequence connection between folds. While there is ample experimental evidence for the existence of super-folds, evidence for a super-network is just starting to emerge. The prediction of a sequence barrier is an intriguing characteristic of sequence space, suggesting that the overall sequence space may be disconnected. The implications and limitations of these observations for evolution of protein structures are discussed.

Indexed as

Models, MolecularProtein FoldingAmino Acid SequenceEvolution, MolecularMutationProtein ConformationProteinsProteinscontact energiesfoldable sequenceslattice modelsmutationsprotein evolution

Identifiers

PMID22095563
PMCPMC3290721

What OpenQuestion holds

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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.