Evidence map›Paper›PMID 12931000›Full record

ArticleProtein science : a publication of the Protein Society2003

Rationally selected basis proteins: a new approach to selecting proteins for spectroscopic secondary structure analysis.

Keith A Oberg, Jean-Marie Ruysschaert, Erik Goormaghtigh

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

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  5. A convenient protein library for spectroscopic calibrations.Computational and structural biotechnology journal · 2020
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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.

Keith A ObergStructural Biology and Bioinformatics Center, Structure and Function of Biological Membranes Laboratory, Free University of Brussels (ULB), B-1050 Brussels, Belgium.
Jean-Marie Ruysschaert
Erik Goormaghtigh

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein basis sets have been extensively used as reference data for the determination of protein structure with optical methods such as circular dichroism and infrared spectroscopies. We have taken a new approach to basis protein selection by utilizing three crystal structure classification databases: CATH, SCOP, and PDB_SELECT. Through the use of the information available in these and other online resources, we identified 115 commercially available proteins as potential basis set candidates. By carefully screening the quality of the crystal structures and commercial protein preparations, we obtained a final set of 50 rationally selected proteins (RaSP50) that has been optimized for use in spectroscopic protein structure determination studies. These proteins span the full range of known protein folds as well as alpha-helix and beta-sheet contents, and they represent a more comprehensive variety of fold types than any previous reference set. This report includes a detailed presentation of the reasoning behind the rational protein selection process, a description of the properties of the RaSP50 set, and a discussion of the types of structural and spectral variations that are represented in the set.

Indexed as

Circular DichroismComputational BiologyCrystallography, X-RayDatabases as TopicMass SpectrometryPeptidesProtein ConformationProtein Structure, SecondaryProteomicsSoftwareSpectrophotometry, InfraredSpectroscopy, Fourier Transform InfraredStatistics as TopicPeptides

Identifiers

PMID12931000
PMCPMC2323998

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.