Evidence map›Paper›PMID 19899165›Full record

ArticleProteins2010

Computational exploration of the network of sequence flow between protein structures.

Baoqiang Cao, Ron Elber

Abstract read
In one paragraph

Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  2. Review
  3. Reversible switching between two common protein folds in a designed system using only temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Multistep mutational transformation of a protein fold through structural intermediates.Protein science : a publication of the Protein Society · 2018
    Article
  5. Structural metamorphism and polymorphism in proteins on the brink of thermodynamic stability.Protein science : a publication of the Protein Society · 2018
    Review
  6. Article
  7. Article
  8. Article
  9. Comprehensive analysis of sequences of a protein switch.Protein science : a publication of the Protein Society · 2016
    Article
  10. Studying protein fold evolution with hybrids of differently folded homologs.Protein engineering, design & selection : PEDS · 2015
    Article
  11. Two is a pair, three is a network.Biophysical journal · 2015
    Article
  12. Article
  13. A polymetamorphic protein.Protein science : a publication of the Protein Society · 2013
    Article
  14. Article
  15. Article
  16. Proteins that switch folds.Current opinion in structural biology · 2010
    Review
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.

Baoqiang CaoInstitute for Computational Engineering and Sciences, University of Texas at Austin, Austin, Texas 78712, USA.
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

We investigate small sequence adjustments (of one or a few amino acids) that induce large conformational transitions between distinct and stable folds of proteins. Such transitions are intriguing from evolutionary and protein-design perspectives. They make it possible to search for ancient protein structures or to design protein switches that flip between folds and functions. A network of sequence flow between protein folds is computed for representative structures of the Protein Data Bank. The computed network is dense, on an average each structure is connected to tens of other folds. Proteins that attract sequences from a higher than expected number of neighboring folds are more likely to be enzymes and alpha/beta fold. The large number of connections between folds may reflect the need of enzymes to adjust their structures for alternative substrates. The network of the Cro family is discussed, and we speculate that capacity is an important factor (but not the only one) that determines protein evolution. The experimentally observed flip from all alpha to alpha + beta fold is examined by the network tools. A kinetic model for the transition of sequences between the folds (with only protein stability in mind) is proposed. Proteins 2010. (c) 2009 Wiley-Liss, Inc.

Indexed as

Amino Acid SequenceDatabases, ProteinEvolution, MolecularProteinsSequence Analysis, ProteinProteins

Identifiers

PMID19899165
PMCPMC2811751

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.