Evidence map›Paper›PMID 29320697›Full record

ArticleBiophysical journal2018

Effects of pH and Salt Concentration on Stability of a Protein G Variant Using Coarse-Grained Models.

Vinícius Martins de Oliveira, Vinícius de Godoi Contessoto, Fernando Bruno da Silva, Daniel Lucas Zago Caetano, Sidney Jurado de Carvalho, Vitor Barbanti Pereira Leite

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
    Review
  5. Article
  6. Article
  7. Mapping the energy landscape of a fold-switching protein MAD2.Protein science : a publication of the Protein Society · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Energy Transport alongMaterials (Basel, Switzerland) · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

6 authors.

Vinícius Martins de OliveiraSão Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences (Ibilce), Campus São José do Rio Preto, Brazil.
Vinícius de Godoi ContessotoSão Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences (Ibilce), Campus São José do Rio Preto, Brazil; Brazilian Bioethanol Science and Technology Laboratory- (CTBE), Campinas, Brazil.
Fernando Bruno da SilvaSão Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences (Ibilce), Campus São José do Rio Preto, Brazil.
Daniel Lucas Zago CaetanoSão Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences (Ibilce), Campus São José do Rio Preto, Brazil.
Sidney Jurado de CarvalhoSão Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences (Ibilce), Campus São José do Rio Preto, Brazil.
Vitor Barbanti Pereira LeiteSão Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences (Ibilce), Campus São José do Rio Preto, Brazil. Electronic address: vleite@sjrp.unesp.br.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The importance of charge-charge interactions in the thermal stability of proteins is widely known. pH and ionic strength play a crucial role in these electrostatic interactions, as well as in the arrangement of ionizable residues in each protein-folding stage. In this study, two coarse-grained models were used to evaluate the effect of pH and salt concentration on the thermal stability of a protein G variant (1PGB-QDD), which was chosen due to the quantity of experimental data exploring these effects on its stability. One of these coarse-grained models, the TKSA, calculates the electrostatic free energy of the protein in the native state via the Tanford-Kirkwood approach for each residue. The other one, CpHMD-SBM, uses a Coulomb screening potential in addition to the structure-based model C

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceBacterial ProteinsDose-Response Relationship, DrugHydrogen-Ion ConcentrationOsmolar ConcentrationProtein ConformationProtein StabilityProtonsSaltsStatic ElectricityBacterial ProteinsIgG Fc-binding protein, StreptococcusProtonsSalts

Identifiers

PMID29320697
PMCPMC5984902

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.