Evidence map›Paper›PMID 21609856›Full record

ArticleMethods in enzymology2009

Fluorescence spectroscopy in thermodynamic and kinetic analysis of pH-dependent membrane protein insertion.

Alexey S Ladokhin

Abstract read
In one paragraph

Article in Methods in enzymology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

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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

1 author.

Alexey S LadokhinDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas, USA.

Funding

pH-Triggered Membrane Insertion of ProteinsR01GM069783 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI COCCO, MELANIE J, KURNIKOVA, MARIA G · 2004 to 2014
$2.5M
NIGMS NIH HHS GM-069783NIGMS NIH HHS R01 GM069783
6 · The paper itself

Abstract

Experimental determination of the free energy stabilizing the structure of membrane proteins in their native lipid environment is undermined by a lack of appropriate methods and suitable model systems. Here, we demonstrate how fluorescence correlation spectroscopy can be used to characterize thermodynamics of pH-triggered bilayer insertion of nonconstitutive membrane proteins (e.g., bacterial toxins, colicins). The experimental design is guided by the appropriate thermodynamic scheme which considers two independent processes: pH-dependent formation of a membrane-competent form and its insertion into the lipid bilayer. Measurements of a model protein annexin B12 under conditions of lipid saturation demonstrate that protonation leading to the formation of the membrane-competent state occurs near membrane interface. Lipid titration experiments demonstrate that the free energy of transfer to the intermediate interfacial state is especially favorable, while the free energy of final insertion is modulated by interplay of hydrophobic and electrostatic interactions on the bilayer interface. The general principles of kinetic measurements along the insertion pathway containing interfacial intermediate are discussed and practical examples emphasizing appropriate fitting and normalization procedures are presented.

Indexed as

ThermodynamicsAnimalsAnnexinsCell MembraneHumansHydrogen-Ion ConcentrationKineticsMembrane ProteinsModels, MolecularProtein FoldingProtein Processing, Post-TranslationalSpectrometry, FluorescenceAnnexinsMembrane Proteins

Identifiers

PMID21609856
PMCPMC4922797

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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.