Unknown

Dataset Information

0

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


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?. 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.

SUBMITTER: Martins de Oliveira V 

PROVIDER: S-EPMC5984902 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Martins de Oliveira Vinícius V   Godoi Contessoto Vinícius de V   Bruno da Silva Fernando F   Zago Caetano Daniel Lucas DL   Jurado de Carvalho Sidney S   Pereira Leite Vitor Barbanti VB  

Biophysical journal 20180101 1


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 ef  ...[more]

Similar Datasets

| S-EPMC4706082 | biostudies-literature
| S-EPMC6342926 | biostudies-literature
| S-EPMC7210967 | biostudies-literature
| S-EPMC5238951 | biostudies-literature
| S-EPMC5649594 | biostudies-literature
| S-EPMC2822134 | biostudies-literature
| S-EPMC2735960 | biostudies-literature
| S-EPMC6331618 | biostudies-literature
| S-EPMC8631167 | biostudies-literature
| S-EPMC3248023 | biostudies-other