Advanced search
Start date
Betweenand

Solvent effects on protein folding thermodynamics

Grant number: 20/04549-0
Support Opportunities:Scholarships in Brazil - Doctorate
Effective date (Start): June 01, 2020
Status:Discontinued
Field of knowledge:Physical Sciences and Mathematics - Chemistry - Physical-Chemistry
Principal Investigator:Leandro Martinez
Grantee:Ander Francisco Pereira
Host Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
Associated research grant:13/08293-7 - CCES - Center for Computational Engineering and Sciences, AP.CEPID
Associated scholarship(s):23/02071-4 - Effects of cosolvents on the folding and function of riboswitches, BE.EP.DR

Abstract

The structure of proteins and their folding mechanisms are dependent on the molecular environment. Proteins can assume distinct conformations, which might be active or inactive, or even assume different functionalities, as a function of the temperature, pressure, or of the properties of solvent in which they are immersed. Proteins assume their function predominantly in aqueous media. However, even in cellular environments many other species exist, such as cosolvents and ions, of which the function of the proteins are ultimately dependent. Some cosolvents are, furthermore, used in vitro for the stabilization of the protein structures and the enhancement of the protein activity in controlled media, envisaging their optimization for specific technological applications. In this project, we will study how different solvents affect the thermodynamics of the folding process of proteins. The folding mechanisms will be obtained using computer simulations of structure-based models. These models consist of simplified representations of the molecular structure with interaction potentials parametrized from the knowledge of native protein structure. Simulations of structure-based models have been shown to accurately reproduce protein folding mechanisms. Once these mechanisms are characterized, all intermediates will be solvated by various solvents and minimum-distance distribution functions, developed in our group, will be used to characterize the solvation structures and the effect of the solvation on the relative stability of the conformers. We expect, then, to reweight the probability of the folding intermediates in each solvent, leading to the description of the thermodynamic effects of solvents on the folding mechanisms. (AU)

News published in Agência FAPESP Newsletter about the scholarship:
Articles published in other media outlets (0 total):
More itemsLess items
VEICULO: TITULO (DATA)
VEICULO: TITULO (DATA)

Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
PEREIRA, ANDER F.; PICCOLI, VINICIUS; MARTINEZ, LEANDRO. Trifluoroethanol direct interactions with protein backbones destabilize a-helices. JOURNAL OF MOLECULAR LIQUIDS, v. 365, p. 11-pg., . (20/04549-0, 20/04916-3, 18/14274-9, 18/24293-0, 13/08293-7, 10/16947-9)

Please report errors in scientific publications list using this form.