Evidence map›Paper›PMID 37415516›Full record

ArticleApplied spectroscopy2023

Ultraviolet Resonance Raman Spectra of Serum Albumins.

Cecilia Spedalieri, Julian Plaickner, Eugen Speiser, Norbert Esser, Janina Kneipp

Open access · hybridAbstract read
In one paragraph

Article in Applied spectroscopy, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.2field-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

4 citing papers in PubMed, 14 citations in OpenAlex.

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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

5 authors at 3 institutions in 1 country.

Cecilia SpedalieriDepartment of Chemistry, Humboldt-Universität zu Berlin, Berlin, Germany.ORCID 0000-0001-7480-0404
Julian PlaicknerTechnische Universität Berlin, Institut für Festkörperphysik, Berlin, Germany.
Eugen SpeiserLaytec AG, Berlin, Germany.
Norbert EsserTechnische Universität Berlin, Institut für Festkörperphysik, Berlin, Germany.
Janina KneippDepartment of Chemistry, Humboldt-Universität zu Berlin, Berlin, Germany.ORCID 0000-0001-8542-6331
Humboldt-Universität zu Berlin · DELeibniz Institute for Analytical Sciences - ISAS · DETechnische Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ultraviolet resonance Raman (UVRR) spectra of the two proteins bovine serum albumin (BSA) and human serum albumin (HSA) in an aqueous solution are compared with the aim to distinguish between them based on their very similar amino acid composition and structure and to obtain signals from tryptophan that has only very few residues. Comparison of the protein spectra with solutions of tryptophan, tyrosine, and phenylalanine in comparative ratios as in the two proteins shows that at an excitation wavelength of 220 nm, the spectra are dominated by the strong resonant contribution from these three amino acids. While the strong enhancement of two and one single tryptophan residue in BSA and HSA, respectively, results in pronounced bands assigned to fundamental vibrations of tryptophan, its weaker overtones and combination bands do not play a major role in the spectral range above 1800 cm

Indexed as

Serum AlbuminTryptophanHumansPhenylalanineSerum Albumin, BovineSpectrum Analysis, RamanTyrosineVibrationPhenylalanineSerum AlbuminSerum Albumin, BovineTryptophanTyrosine220 nmbovine serum albuminBSAHSAHuman serum albuminphenylalaninetryptophantyrosineultraviolet resonance RamanUVRR

Identifiers

PMID37415516
PMCPMC10478327
OpenAlexW4383482531

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.