Evidence map›Paper›PMID 31588326›Full record

ArticleChemical science2019

Structure and effective charge characterization of proteins by a mobility capillary electrophoresis based method.

Wenjing Zhang, Haimei Wu, Rongkai Zhang, Xiang Fang, Wei Xu

Abstract read
In one paragraph

Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Advancement of microchip electrophoresis coupled with capacitively coupled contactless conductivity detection-from design to application (2018-2024).Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Review
  2. Review
  3. Article
  4. Recent (2018-2020) development in capillary electrophoresis.Analytical and bioanalytical chemistry · 2022
    Review
  5. Measuring how two proteins affect each other's net charge in a crowded environment.Protein science : a publication of the Protein Society · 2021
    Article
  6. Article
  7. Article
  8. Article
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

5 authors.

Wenjing ZhangSchool of Life Science , Beijing Institute of Technology , No. 5 South Zhongguancun Street, Haidian Dist , Beijing , China . Email: weixu@bit.edu.cn.ORCID 0000-0003-4968-6413
Haimei WuSchool of Life Science , Beijing Institute of Technology , No. 5 South Zhongguancun Street, Haidian Dist , Beijing , China . Email: weixu@bit.edu.cn.
Rongkai ZhangSchool of Life Science , Beijing Institute of Technology , No. 5 South Zhongguancun Street, Haidian Dist , Beijing , China . Email: weixu@bit.edu.cn.
Xiang FangNational Institute of Metrology , No. 18, Bei San Huan Dong Lu, Chaoyang Dist , Beijing , China.
Wei XuSchool of Life Science , Beijing Institute of Technology , No. 5 South Zhongguancun Street, Haidian Dist , Beijing , China . Email: weixu@bit.edu.cn.ORCID 0000-0001-5274-1546

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Measuring the conformations and effective charges of proteins in solution is critical for investigating protein bioactivity, but their rapid analysis remains a challenging problem. Here we report a mobility capillary electrophoresis (MCE) based method for the rapid analysis of protein stereo-structures and effective charges in different solution environments. With the capability of mixture separation, MCE measures the hydrodynamic radius of a protein through Taylor dispersion analysis and its effective charge through ion mobility analysis. The experimental results acquired from MCE are then utilized to restrain molecular dynamics simulations, so that the most probable conformation of that protein can be obtained. As proof-of-concept demonstrations, the charge states and structures of five proteins were analyzed under close to native environments. The conformation transitions and charge state variations of bovine serum albumin and lysozyme under different pH conditions were also investigated. This method is promising for high-throughput protein analysis, which could potentially be coupled with mass spectrometry for investigating protein stereo-structures and functions in top-down proteomics.

Identifiers

PMID31588326
PMCPMC6761862

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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.