Evidence map›Paper›PMID 19923435›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Conformations and free energy landscapes of polyproline peptides.

Mahmoud Moradi, Volodymyr Babin, Christopher Roland, Thomas A Darden, Celeste Sagui

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Review
  2. Energy landscape analysis of the development of the chromosome structure across the cell cycle.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. An Unbound Proline-Rich Signaling Peptide Frequently SamplesFrontiers in molecular biosciences · 2021
    Article
  11. Article
  12. Article
  13. Investigation of theRSC advances · 2020
    Article
  14. Energy Landscapes of Deoxyxylo- and Xylo-Nucleic Acid Octamers.The journal of physical chemistry. B · 2020
    Article
  15. A spin-1 representation for dual-funnel energy landscapes.The Journal of chemical physics · 2018
    Article
  16. Article
  17. Article
  18. Infrared Multiple-Photon Dissociation Action Spectroscopy of the bJournal of the American Society for Mass Spectrometry · 2017
    Article
  19. Article
  20. Measuring the Elasticity of Poly-l-Proline Helices with Terahertz Spectroscopy.Angewandte Chemie (International ed. in English) · 2016
    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

5 authors.

Mahmoud MoradiCenter for High Performance Simulations and Department of Physics, North Carolina State University, Raleigh, NC 27695, USA.
Volodymyr Babin
Christopher Roland
Thomas A Darden
Celeste Sagui

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of the proline amino acid allows folded polyproline peptides to exist as both left- (PPII) and right-handed (PPI) helices. We have characterized the free energy landscapes of hexamer, nanomer, and tridecamer polyproline peptides in gas phase and implicit water as well as explicit hexane and 1-propanol for the nanomer. To enhance the sampling provided by regular molecular dynamics, we used the recently developed adaptively biased molecular dynamics method, which describes Landau free energy maps in terms of relevant collective variables. These maps, as a function of the collective variables of handedness, radius of gyration, and three others based on the peptide torsion angle omega, were used to determine the relative stability of the different structures, along with an estimate of the transition pathways connecting the different minima. Results show the existence of several metastable isomers and therefore provide a complementary view to experimental conclusions based on photo-induced electron transfer experiments with regard to the existence of stable heterogeneous subpopulations in PPII polyproline.

Indexed as

PeptidesProtein ConformationThermodynamicsPeptidespolyproline

Identifiers

PMID19923435
PMCPMC2791577

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.