Evidence map›Paper›PMID 18330556›Full record

ArticleEuropean biophysics journal : EBJ2008

Water structure around dipeptides in aqueous solutions.

Sylvia E McLain, Alan K Soper, Anthony Watts

Abstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
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

7 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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

3 authors at 3 institutions in 2 countries.

Sylvia E McLainNeutron Scattering Sciences Division and Center for Molecular Biophysics, Oak Ridge National Laboratory, P.O Box 2008, Oak Ridge, TN 37831-6475, USA. mclainse@ornl.gov
Alan K Soper
Anthony Watts
Oak Ridge National Laboratory · USRutherford Appleton Laboratory · GBUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bulk water structure around small peptide fragments--glycyl-L-alanine, glycyl-L-proline and L:-alanyl-L-proline-has been determined by a combination of neutron diffraction with isotopic substitution and empirical potential structural refinement techniques. The addition of each of the dipeptides to water gives rise to decreased water-water coordination in the surrounding water solvent. Additionally, both the Ow-Ow radial distribution functions and the water-water spatial density functions in all of the solutions indicate an electrostrictive effect in the second water coordination shell of the bulk water network. This effect is not observed in similar experiments on the amino acid L: -proline alone in solution, which is one component of two of the peptides measured here.

Indexed as

Amino AcidsComputer SimulationDipeptidesHydrophobic and Hydrophilic InteractionsModels, MolecularNeutron DiffractionSolutionsWaterAmino AcidsDipeptidesSolutionsWater

Identifiers

PMID18330556
OpenAlexW2031799400

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.