Evidence map›Paper›PMID 15240484›Full record

ArticleBiophysical journal2004

A quantitative XANES analysis of the calcium high-affinity binding site of the purple membrane.

Francesc Sepulcre, M Grazia Proietti, Maurizio Benfatto, Stefano Della Longa, Joaquin García, Esteve Padrós

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 51% 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

3 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Contemporary Use of Anomalous Diffraction in Biomolecular Structure Analysis.Methods in molecular biology (Clifton, N.J.) · 2017
    Review
  3. 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

6 authors at 5 institutions in 2 countries.

Francesc SepulcreDepartament d'Enginyeria Agroalimentària i Biotecnologia, Escola Superior d'Agricultura, Universitat Politècnica de Catalunya, Barcelona, Spain. francesc.sepulcre@upc.es
M Grazia Proietti
Maurizio Benfatto
Stefano Della Longa
Joaquin García
Esteve Padrós
Universidad de Zaragoza · ESIstituto Nazionale di Fisica Nucleare, Laboratori Nazionali di Frascati · ITUniversitat Autònoma de Barcelona · ESUniversitat Politècnica de Catalunya · ESUniversity of L'Aquila · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this article we report x-ray absorption measurements of Ca(2+)-substituted bacteriorhodopsin. We present a detailed study of the absorption spectrum close to the absorption edge that is very sensitive to the site geometry. We combined ab initio calculations of the x-ray absorption cross section based on a full multiple scattering approach, with a best fit of the experimental data performed by changing the cluster geometry. The Ca(2+)-bacteriorhodopsin environment is composed of six oxygen atoms showing a distorted orthorhombic symmetry, whereas the Ca(2+) in water solution has a regular octahydrated first sphere of coordination. Our results are in good agreement with previous molecular models suggesting that the high-affinity cationic site could be in the proximity of the retinal pocket. Our results provide strong direct evidence of the specific binding site of the metal cation in bacteriorhodopsin.

Indexed as

Models, MolecularAbsorptiometry, PhotonBacteriorhodopsinsBinding SitesCalciumHalobacterium salinarumOxygenPurple MembraneBacteriorhodopsinsCalciumOxygen

Identifiers

PMID15240484
PMCPMC1304372
OpenAlexW2085952071

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.