Evidence map›Paper›PMID 11847268›Full record

ArticleProtein science : a publication of the Protein Society2002

Detecting equilibrium cytochrome c folding intermediates by electrospray ionisation mass spectrometry: two partially folded forms populate the molten-globule state.

Rita Grandori

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

18 citing papers in PubMed, 91 citations in OpenAlex.

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  6. Mass spectrometry-based methods to study protein architecture and dynamics.Protein science : a publication of the Protein Society · 2013
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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 at 1 institution in 1 country.

Rita GrandoriInstitute of Chemistry, Johannes Kepler University, A-4040 Linz, Austria. rita.grandori@jku.at
Johannes Kepler University of Linz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nanoelectrospray ionization mass spectrometry (nano-ESI-MS) is applied to the characterization of ferric cytochromec (cytc) conformational states under different solvent conditions. The methanol-induced molten-globule state in the pH range 2.6-3.0 is found to be populated by two distinct, partially folded conformers I(A) and I(B). The more compact intermediate I(B) resembles that induced by glycerol in acid-unfolded cytc. The less compact one, I(A), also can be induced by destabilization of the native structure by trifluoroethanol. I(A) and I(B) can be detected, in the absence of additives, around the midpoint of the acid-induced unfolding transition, providing direct evidence for involvement of equilibrium folding intermediates in cytc conformational transitions at low pH. This study shows that mass spectrometry can contribute to the characterization of molten-globule states of proteins by detection of distinct, although poorly populated, conformations involved in a dynamic equilibrium.

Indexed as

Protein FoldingSpectrometry, Mass, Electrospray IonizationCytochrome c GroupMethanolProtein ConformationTrifluoroethanolCytochrome c GroupMethanolTrifluoroethanol

Identifiers

PMID11847268
PMCPMC2373474
OpenAlexW2094150300

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.