| Full text | |
| Author(s): |
Contessoto, Vinicius G.
[1]
;
Ferreira, Paulo H. B.
[2]
;
Chahine, Jorge
[1]
;
Leite, Vitor B. P.
[1]
;
Oliveira, Ronaldo J.
[2]
Total Authors: 5
|
| Affiliation: | [1] Sao Paulo State Univ, Dept Phys, Inst Biosci Letters & Exact Sci, BR-15054000 Sao Jose Do Rio Preto - Brazil
[2] Univ Fed Triangulo Mineiro, Lab Biofis Teor, Dept Fis, Inst Cincias Exatas Nat & Educ, BR-38064200 Uberaba - Brazil
Total Affiliations: 2
|
| Document type: | Journal article |
| Source: | Journal of Physical Chemistry B; v. 125, n. 42, p. 11673-11686, OCT 28 2021. |
| Web of Science Citations: | 0 |
| Abstract | |
Molecular crowding is a ubiquitous phenomenon in biological systems, with significant consequences on protein folding and stability. Small compounds, such as the osmolyte trimethylamine N-oxide (TMAO), can also present similar effects. To analyze the effects arising from these solute-like molecules, we performed a series of crowded coarse-grained folding simulations. Two well-known proteins were chosen, CI2 and SH3, modeled by the alpha-carbon-structure-based model. In the simulations, the crowding molecules were represented by low-sized neutral atom beads in different concentrations. The results show that a low level of the volume fraction occupied by neutral agents can change protein stability and folding kinetics for the two systems. However, the kinetics were shown to be unaffected in their respective folding temperatures. The faster kinetics correlates with changes in the folding route for systems at the same temperature, where non-native contacts were shown to be relevant. The transition states of the two systems with and without crowders are similar. In the case of SH3, there are differences in the structuring of two strands, which may be associated with the increase in its folding rate, in addition to the destabilization of the denatured ensemble. The present study also detected a crossover in the thermodynamic stability behavior, previously observed experimentally and theoretically. As the temperature increases, crowders change from destabilizing to stabilizing agents. (AU) | |
| 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 Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 19/22540-3 - Studies of energy landscapes of biological macromolecules |
| Grantee: | Vitor Barbanti Pereira Leite |
| Support Opportunities: | 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 Opportunities: | Regular Research Grants |