Evidence map›Paper›PMID 15007694›Full record

ReviewThe European physical journal. E, Soft matter2003

Low-temperature behavior of water confined by biological macromolecules and its relation to protein dynamics.

M Weik

Abstract readReview
PubMed Publisher
In one paragraph

Review in The European physical journal. E, Soft matter, 2003. 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
–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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Entrapment of water by subunit c of ATP synthase.Journal of the Royal Society, Interface · 2008
    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

1 author.

M WeikLaboratoire de Biophysique Moléculaire, Institut de Biologie Structurale, 41 rue Jules Horowitz, 38027, Grenoble Cedex 1, France. weik@ibs.fr

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Confined water is an essential component of biological entities and processes and its properties differ from the ones of bulk water. Since protein and water dynamics are thought to be strongly coupled, and since macromolecular dynamics is crucial for biological function, the study of water confined by biological macromolecules is not only interesting on its own right but often provides useful information for understanding biological activity at the molecular level. Studies are reviewed that focus on the low-temperature behavior of water confined in protein crystals and in stacks of native biological membranes. Diffraction methods allowed the determination of characteristic changes that relate to the glass transition and crystallization of water. Protein crystallography and energy-resolved neutron scattering are employed to gain further insight into the coupling of solvent and protein dynamics.

Indexed as

Models, MolecularBacteriorhodopsinsBiopolymersFreezingMacromolecular SubstancesPowdersProtein BindingProtein ConformationProteinsPurple MembraneTemperatureWaterBacteriorhodopsinsBiopolymersMacromolecular SubstancesPowdersProteinsWater

Identifiers

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.