Evidence map›Paper›PMID 19570795›Full record

ArticleJournal of the Royal Society, Interface2009

Combining structure and dynamics: non-denaturing high-pressure effect on lysozyme in solution.

Maria Grazia Ortore, Francesco Spinozzi, Paolo Mariani, Alessandro Paciaroni, Leandro R S Barbosa, Heinz Amenitsch, Milos Steinhart, Jacques Ollivier, Daniela Russo

Abstract read
In one paragraph

Article in Journal of the Royal Society, Interface, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Fast calculation of small-angle scattering profiles of dense protein solutions modeled at the all-atom level.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Unravelling the Adaptation Mechanisms to High Pressure in Proteins.International journal of molecular sciences · 2022
    Article
  4. Taurine Stabilizing Effect on Lysozyme.Life (Basel, Switzerland) · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Gelling without Structuring: A SAXS Study of the Interactions among DNA Nanostars.Langmuir : the ACS journal of surfaces and colloids · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Pressure effects on collective density fluctuations in water and protein solutions.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Extreme biophysics: Enzymes under pressure.Journal of computational chemistry · 2017
    Article
  17. Article
  18. Review
  19. Proteins in binary solvents.Biophysical reviews · 2016
    Review
  20. 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

9 authors.

Maria Grazia OrtoreDipartimento SAIFET, Sezione Scienze Fisiche, Università Politecnica delle Marche and CNISM, Ancona, Italy. mg.ortore@alisf1.univpm.it; russo@ill.fr
Francesco Spinozzi
Paolo Mariani
Alessandro Paciaroni
Leandro R S Barbosa
Heinz Amenitsch
Milos Steinhart
Jacques Ollivier
Daniela Russo

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small-angle X-ray scattering (SAXS) and elastic and quasi-elastic neutron scattering techniques were used to investigate the high-pressure-induced changes on interactions, the low-resolution structure and the dynamics of lysozyme in solution. SAXS data, analysed using a global-fit procedure based on a new approach for hydrated protein form factor description, indicate that lysozyme completely maintains its globular structure up to 1500 bar, but significant modifications in the protein-protein interaction potential occur at approximately 600-1000 bar. Moreover, the mass density of the protein hydration water shows a clear discontinuity within this pressure range. Neutron scattering experiments indicate that the global and the local lysozyme dynamics change at a similar threshold pressure. A clear evolution of the internal protein dynamics from diffusing to more localized motions has also been probed. Protein structure and dynamics results have then been discussed in the context of protein-water interface and hydration water dynamics. According to SAXS results, the new configuration of water in the first hydration layer induced by pressure is suggested to be at the origin of the observed local mobility changes.

Indexed as

SynchrotronsMuramidaseNeutron DiffractionPressureProtein ConformationProtein DenaturationSolutionsStructure-Activity Relationshiphen egg lysozymeMuramidaseSolutions

Identifiers

PMID19570795
PMCPMC2843975

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.