Evidence map›Paper›PMID 31218624›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2019

UV Resonance Raman Spectroscopy as a Tool to Probe Membrane Protein Structure and Dynamics.

DeeAnn K Asamoto, Judy E Kim

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

5 citing papers in PubMed, 11 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

2 authors at 1 institution in 1 country.

DeeAnn K AsamotoDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.
Judy E KimDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA. judyk@ucsd.edu.
University of California, San Diego · US

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
NIGMS NIH HHS T32 GM008326
6 · The paper itself

Abstract

Ultraviolet resonance Raman (UVRR) spectroscopy is a vibrational technique that reveals structures and dynamics of biological macromolecules without the use of extrinsic labels. By tuning the Raman excitation wavelength to the deep UV region (e.g., 228 nm), Raman signal from tryptophan and tyrosine residues are selectively enhanced, allowing for the study of these functionally relevant amino acids in lipid and aqueous environments. In this chapter, we present methods on the UVRR data acquisition and analysis of the tryptophan vibrational modes of a model β-barrel membrane protein, OmpA, in folded and unfolded conformations.

Indexed as

Amino AcidsBacterial Outer Membrane ProteinsLipidsMembrane ProteinsMembranesSpectrophotometry, UltravioletSpectrum Analysis, RamanTryptophanTyrosineVibrationAmino AcidsBacterial Outer Membrane ProteinsLipidsMembrane ProteinsOMPA outer membrane proteinsTryptophanTyrosineLipidsMembrane proteinsSmall unilamellar vesiclesTryptophanUV resonance RamanVibrational spectroscopy

Identifiers

PMID31218624
PMCPMC6874512
OpenAlexW2951354058

What OpenQuestion holds

Textmetadata
LicenceTDM
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.