Evidence map›Paper›PMID 42156682›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Protein-Membrane Interactions Studied by Transmission and Total Internal Reflection FTIR Spectroscopy.

Suren A Tatulian

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Suren A TatulianDepartment of Physics, University of Central Florida, Orlando, FL, USA. statulia@ucf.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fourier transform infrared (FTIR) spectroscopy has become one of the mainstream techniques of structural characterization of proteins, peptides, and protein-membrane interactions. While the method does not have the capability of providing the atomic-resolution structure of proteins or lipids, it is exquisitely sensitive to conformational changes occurring in proteins upon functional transitions or intermolecular interactions. Sensitivity of vibrational frequencies to atomic masses has led to the development of "isotope-edited" FTIR spectroscopy, where structural effects in two proteins, one unlabeled and the other labeled with a heavier stable isotope, such as

Indexed as

Cell MembraneMembrane ProteinsIsotope LabelingProtein BindingSpectroscopy, Fourier Transform InfraredMembrane ProteinsInfrared spectroscopyMembraneProtein isotope labelingProtein–membrane interactionsProtein structureTransmembrane orientation

Identifiers

PMID42156682

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.