Evidence map›Paper›PMID 26840723›Full record

ArticleBiophysical journal2016

Early Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity.

Rita Pancsa, Daniele Raimondi, Elisa Cilia, Wim F Vranken

Abstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Online biophysical predictions for SARS-CoV-2 proteins.BMC molecular and cell biology · 2021
    Article
  5. Review
  6. Interpreting a black box predictor to gain insights into early folding mechanisms.Computational and structural biotechnology journal · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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.

Rita PancsaStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Daniele RaimondiStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Elisa CiliaStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Wim F VrankenStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium. Electronic address: wvranken@vub.ac.be.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein folding is in its early stages largely determined by the protein sequence and complex local interactions between amino acids, resulting in lower energy conformations that provide the context for further folding into the native state. We compiled a comprehensive data set of early folding residues based on pulsed labeling hydrogen deuterium exchange experiments. These early folding residues have corresponding higher backbone rigidity as predicted by DynaMine from sequence, an effect also present when accounting for the secondary structures in the folded protein. We then show that the amino acids involved in early folding events are not more conserved than others, but rather, early folding fragments and the secondary structure elements they are part of show a clear trend toward conserving a rigid backbone. We therefore propose that backbone rigidity is a fundamental physical feature conserved by proteins that can provide important insights into their folding mechanisms and stability.

Indexed as

Molecular Dynamics SimulationProtein FoldingAmino Acid SequenceCytochromes cMolecular Sequence DataProtein BindingProtein ConformationCytochromes c

Identifiers

PMID26840723
PMCPMC4744172

What OpenQuestion holds

Textmetadata
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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.