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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
de Oliveira, Vinicius Martins [1] ; Contessoto, Vinicius de Godoi [2, 1] ; da Silva, Fernando Bruno [1] ; Zago Caetano, Daniel Lucas [1] ; de Carvalho, Sidney Jurado [1] ; Pereira Leite, Vitor Barbanti [1]
Total Authors: 6
Affiliation:
[1] Sao Paulo State Univ UNESP, Inst Biosci Humanities & Exact Sci Ibilce, Campus Sao Jose do Rio Preto, Sao Jose Do Rio Preto, SP - Brazil
[2] Brazilian Bioethanol Sci & Technol Lab CTBE, Campinas, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: BIOPHYSICAL JOURNAL; v. 114, n. 1, p. 65-75, JAN 9 2018.
Web of Science Citations: 8
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 Ca. Both models simulate the system in constant pH. The comparison between the experimental stability analysis and the computational results obtained by these simple models showed a good agreement. Through the TKSA method, the role of each charged residue in the protein's thermal stability was inferred. Using CpHMD-SBM, it was possible to evaluate salt and pH effects throughout the folding process. Finally, the computational pKa values were calculated by both methods and presented a good level of agreement with the experiments. This study provides, to our knowledge, new information and a comprehensive description of the electrostatic contribution to protein G stability. (AU)

FAPESP's process: 17/09662-7 - Rational Evolution by Computational Methods Applied in Enzymes Related to Bioethanol Production
Grantee:Vinícius de Godoi Contessoto
Support type: Scholarships abroad - Research Internship - Post-doctor
FAPESP's process: 13/13151-7 - Study by computational simulation of the interaction between polyelectrolytes and macromolecules with helical charge distribution
Grantee:Daniel Lucas Zago Caetano
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 14/06862-7 - Computational studies in protein folding and enzymes engineering involved in bioethanol production
Grantee:Vitor Barbanti Pereira Leite
Support type: Regular Research Grants
FAPESP's process: 16/19766-1 - Biological macromolecules energy landscapes with applications in biotechnology and in biomedicine
Grantee:Vitor Barbanti Pereira Leite
Support type: Regular Research Grants
FAPESP's process: 16/13998-8 - Rational evolution by computational methods applied to predict mutations in enzymes to biofuels production
Grantee:Vinícius de Godoi Contessoto
Support type: Scholarships in Brazil - Post-Doctorate