Evidence map›Paper›PMID 22571437›Full record

ArticleJournal of biomolecular structure & dynamics2012

Levinthal's question revisited, and answered.

Arieh Ben-Naim

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of biomolecular structure & dynamics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. The fate of proteins in outer space.International journal of astrobiology · 2017
    Article
  10. Paradoxes of early stages of evolution of life and biological complexity.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2015
    Article
  11. Article
  12. Molecular insights into the reversible formation of tau protein fibrils.Chemical communications (Cambridge, England) · 2013
    Article
  13. The unsolved "solved-problem" of protein folding.Journal of biomolecular structure & dynamics · 2013
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

Arieh Ben-NaimDepartment of Physical Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, Jerusalem, 91904, Israel. arieh@fh.huji.ac.il

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Attempts to answer the Levinthal question "How proteins fold to give such a unique structure" are discussed. In the first part of this article, we focus on a few reasons as to why the solution to the protein-folding problem (PFP) has been elusive for a very long time. One is a result of the misinterpretation of Anfinsen's Thermodynamic hypothesis which led to the conclusion that the native structure of a protein must be at a global minimum of the Gibbs energy. The second is the result of the adherence to the hydrophobic paradigm, and at the same time ignoring a whole repertoire of hydrophilic effects. It is argued that switching from a target-based to a caused-based approach, and adopting the hydrophilic paradigm leads straightforwardly to a simple answer to Levinthal's question, as well as to a solution of the PFP.

Indexed as

Protein ConformationProtein FoldingHydrophobic and Hydrophilic InteractionsModels, TheoreticalProteinsThermodynamicsProteins

Identifiers

PMID22571437

What OpenQuestion holds

Textmetadata
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.