Evidence map›Paper›PMID 24038622›Full record

ArticleProtein science : a publication of the Protein Society2013

Mechanistic investigation of domain specific unfolding of human serum albumin and the effect of sucrose.

Rajeev Yadav, Pratik Sen

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

3 citing papers in PubMed, 33 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.

Rajeev YadavDepartment of Chemistry, Indian Institute of Technology Kanpur, Kanpur, 208 016, Uttar Pradesh, India.
Pratik Sen
Indian Institute of Technology Kanpur · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study is devoted to understand the unfolding mechanism of a multidomain protein, human serum albumin (HSA), in absence and presence of the sucrose by steady-state and time-resolved fluorescence spectroscopy with domain specific marker molecules and is further being substantiated by molecular dynamics (MD) simulation. In water, the domain III of HSA found to unfold first followed by domains I and II as the concentration of GnHCl is increased in the medium. The sequential unfolding behavior of different domains of HSA remains same in presence of sucrose; however, a higher GnHCl concentration is required for unfolding, suggesting stabilizing effect of sucrose on HSA. Domain I is found to be most stabilized by sucrose. The stabilization of domain II is somewhat similar to domain I, but the effect of sucrose on domain III is found to be very small. MD simulation also predicted a similar behavior of sucrose on HSA. The stabilizing effect of sucrose is explained in terms of the entrapment of water molecules in between HSA surface and sucrose layer as well as direct interaction between HSA and sucrose.

Indexed as

Protein UnfoldingAnilino NaphthalenesulfonatesAnimalsCircular DichroismGuanidineHeminHumansModels, MolecularMolecular Dynamics SimulationProtein DenaturationProtein StabilityProtein Structure, TertiarySerum AlbuminSpectrometry, FluorescenceSucroseTryptophan8-anilino-1-naphthalenesulfonic acidAnilino NaphthalenesulfonatesGuanidineHeminSerum AlbuminSucroseTryptophanWaterdenaturationhuman serum albuminmultidomain proteinstabilizationsugarunfolding mechanism

Identifiers

PMID24038622
PMCPMC3831672
OpenAlexW2106223561

What OpenQuestion holds

Textmetadata
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.