Evidence map›Paper›PMID 16249331›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

A geometric construction determines all permissible strand arrangements of sandwich proteins.

A S Fokas, T S Papatheodorou, A E Kister, I M Gelfand

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Rules for connectivity of secondary structure elements in protein: Two-layer αβ sandwiches.Protein science : a publication of the Protein Society · 2017
    Article
  2. Article
  3. ASTRO-FOLD 2.0: an Enhanced Framework for Protein Structure Prediction.AIChE journal. American Institute of Chemical Engineers · 2012
    Article
  4. Article
  5. Article
  6. Strict rules determine arrangements of strands in sandwich proteins.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

4 authors.

A S FokasDepartment of Applied Mathematics and Theoretical Physics, University of Cambridge, Cambridge CB3 0WA, United Kingdom. t.fokas@damtp.cam.ac.uk
T S Papatheodorou
A E Kister
I M Gelfand

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For a large class of proteins called sandwich-like proteins (SPs), the secondary structures consist of two beta-sheets packed face-to-face, with each beta-sheet consisting typically of three to five beta-strands. An important step in the prediction of the three-dimensional structure of a SP is the prediction of its supersecondary structure, namely the prediction of the arrangement of the beta-strands in the two beta-sheets. Recently, significant progress in this direction was made, where it was shown that 91% of observed SPs form what we here call "canonical motifs." Here, we show that all canonical motifs can be constructed in a simple manner that is based on thermodynamic considerations and uses certain geometric structures. The number of these structures is much smaller than the number of possible strand arrangements. For instance, whereas for SPs consisting of six strands there exist a priori 900 possible strand arrangements, there exist only five geometric structures. Furthermore, the few motifs that are noncanonial can be constructed from canonical motifs by a simple procedure.

Indexed as

Amino Acid MotifsModels, MolecularProtein ConformationProteinsProtein Structure, SecondaryThermodynamicsProteins

Identifiers

PMID16249331
PMCPMC1276083

What OpenQuestion holds

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Registered trials

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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.