Evidence map›Paper›PMID 34845607›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Measurement of Submillisecond Protein Folding Using Trp Fluorescence and Photochemical Oxidation.

David Witalka, Lisa J Lapidus

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. 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
1.2field-weighted citation impact, top 19% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

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

2 authors at 1 institution in 1 country.

David WitalkaDepartment of Physics and Astronomy, Michigan State University, East Lansing, MI, USA.
Lisa J LapidusDepartment of Physics and Astronomy, Michigan State University, East Lansing, MI, USA. lapidus@msu.edu.
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Observation of protein folding on submillisecond time scales requires specialized ultra-rapid mixers coupled to optical or chemical probes. Here we describe the protocol for employing a microfabricated mixer with a mixing time of 8 μs coupled to a UV confocal microscope. This instrument can detect Trp fluorescence and also excite hydroxyl radicals that label the folding protein which can be detected by mass spectrometry.

Indexed as

Protein FoldingHydroxyl RadicalMass SpectrometryOxidation-ReductionHydroxyl RadicalFast photochemical oxidation of proteins (FPOP)Microfluidic mixerProtein foldingTrp fluorescence

Identifiers

PMID34845607
OpenAlexW3214920041

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.