Evidence map›Paper›PMID 21376059›Full record

ArticleJournal of molecular biology2011

Characterizing the existing and potential structural space of proteins by large-scale multiple loop permutations.

Liang Dai, Yaoqi Zhou

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Folds from fold: Exploring topological isoforms of a single-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Rules for connectivity of secondary structure elements in protein: Two-layer αβ sandwiches.Protein science : a publication of the Protein Society · 2017
    Article
  7. Article
  8. Article
  9. Biophysics of protein evolution and evolutionary protein biophysics.Journal of the Royal Society, Interface · 2014
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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.

Liang DaiSchool of Informatics, Indiana University Purdue University Indianapolis, and Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, 719 Indiana Avenue, Walker Plaza Building Suite 319, Indianapolis, IN 46202, USA.
Yaoqi Zhou

Funding

Toward experimental quality protein structures: a synergistic approachR01GM067168 · NIGMS · UNIVERSITY OF DELAWARE · PI DUAN, YONG, ZHOU, YAOQI · 2003 to 2012
$2.4M
Statistical Energy Functions: a Fragment-based ApproachR01GM085003 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI ZHOU, YAOQI · 2008 to 2011
$1.1M
NIGMS NIH HHS GM R01 085003NIGMS NIH HHS R01 GM067168NIGMS NIH HHS R01 GM085003
6 · The paper itself

Abstract

Worldwide structural genomics projects are increasing structure coverage of sequence space but have not significantly expanded the protein structure space itself (i.e., number of unique structural folds) since 2007. Discovering new structural folds experimentally by directed evolution and random recombination of secondary-structure blocks is also proved rarely successful. Meanwhile, previous computational efforts for large-scale mapping of protein structure space are limited to simple model proteins and led to an inconclusive answer on the completeness of the existing observed protein structure space. Here, we build novel protein structures by extending naturally occurring circular (single-loop) permutation to multiple loop permutations (MLPs). These structures are clustered by structural similarity measure called TM-score. The computational technique allows us to produce different structural clusters on the same naturally occurring, packed, stable core but with alternatively connected secondary-structure segments. A large-scale MLP of 2936 domains from structural classification of protein domains reproduces those existing structural clusters (63%) mostly as hubs for many nonredundant sequences and illustrates newly discovered novel clusters as islands adopted by a few sequences only. Results further show that there exist a significant number of novel potentially stable clusters for medium-size or large-size single-domain proteins, in particular, >100 amino acid residues, that are either not yet adopted by nature or adopted only by a few sequences. This study suggests that MLP provides a simple yet highly effective tool for engineering and design of novel protein structures (including naturally knotted proteins). The implication of recovering new-fold targets from critical assessment of structure prediction techniques (CASP) by MLP on template-based structure prediction is also discussed. Our MLP structures are available for download at the publication page of the Web site http://sparks.informatics.iupui.edu.

Indexed as

Cluster AnalysisComputational BiologyModels, MolecularProtein EngineeringProtein FoldingProteinsProtein Structure, SecondaryProtein Structure, TertiaryProteins

Identifiers

PMID21376059
PMCPMC3075335

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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.