Evidence map›Paper›PMID 33831390›Full record

ArticleBiophysical journal2021

Electrostatic interaction optimization improves catalytic rates and thermotolerance on xylanases.

Vinícius de Godoi Contessoto, Felipe Cardoso Ramos, Ricardo Rodrigues de Melo, Vinícius Martins de Oliveira, Josiane Aniele Scarpassa, Amanda Silva de Sousa, Letıcia Maria Zanphorlin, Gabriel Gouvea Slade, Vitor Barbanti Pereira Leite, Roberto Ruller

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

2 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. 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

10 authors at 5 institutions in 2 countries.

Vinícius de Godoi ContessotoBrazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, São Paulo, Brazil; Center for Theoretical Biological Physics, Rice University, Houston, Texas; Department of Physics, Institute of Biosciences, Letters and Exact Sciences, São Paulo State University, São José do Rio Preto, São Paulo, Brazil.
Felipe Cardoso RamosBrazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, São Paulo, Brazil.
Ricardo Rodrigues de MeloBrazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, São Paulo, Brazil.
Vinícius Martins de OliveiraBrazilian Biosciences National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, São Paulo, Brazil.
Josiane Aniele ScarpassaBrazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, São Paulo, Brazil.
Amanda Silva de SousaBrazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, São Paulo, Brazil.
Letıcia Maria ZanphorlinBrazilian Biorenewables National Laboratory, Brazilian Center for Research in Energy and Materials, Campinas, São Paulo, Brazil.
Gabriel Gouvea SladeTheoretical Biophysics Laboratory, Institute of Exact Sciences, Natural and Education, Federal University of Triângulo Mineiro, Uberaba, Minas Gerais, Brazil.
Vitor Barbanti Pereira LeiteDepartment of Physics, Institute of Biosciences, Letters and Exact Sciences, São Paulo State University, São José do Rio Preto, São Paulo, Brazil. Electronic address: vitor.leite@unesp.br.
Roberto RullerMicroorganisms and General Biochemistry Laboratory, Institute of Bioscience, Federal University of Mato Grosso do Sul, Campo Grande, Mato Grosso do Sul, Brazil.
Brazilian Center for Research in Energy and Materials · BRCenter for Theoretical Biological Physics · USUniversidade Estadual Paulista (Unesp) · BRUniversidade Federal de Mato Grosso do Sul · BRUniversidade Federal do Triângulo Mineiro · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding the aspects that contribute to improving proteins' biochemical properties is of high relevance for protein engineering. Properties such as the catalytic rate, thermal stability, and thermal resistance are crucial for applying enzymes in the industry. Different interactions can influence those biochemical properties of an enzyme. Among them, the surface charge-charge interactions have been a target of particular attention. In this study, we employ the Tanford-Kirkwood solvent accessibility model using the Monte Carlo algorithm (TKSA-MC) to predict possible interactions that could improve stability and catalytic rate of a WT xylanase (XynA

Indexed as

Endo-1,4-beta XylanasesThermotoleranceEnzyme StabilityProtein EngineeringProteinsStatic ElectricityEndo-1,4-beta XylanasesProteins

Identifiers

PMID33831390
PMCPMC8390807
OpenAlexW3148270819

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.