| Texto completo | |
| Autor(es): |
Sucharski, Fernanda
;
Gallo, Gloria
;
Coelho, Camila
;
Hardy, Leon
;
Wuertele, Martin
Número total de Autores: 5
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Journal of Molecular Modeling; v. 29, n. 5, p. 10-pg., 2023-05-01. |
| Resumo | |
Discerning the determinants of protein thermostability is very important both from the theoretical and applied perspective. Different lines of evidence seem to indicate that a dynamical network of salt bridges/charged residues plays a fundamental role in the thermostability of enzymes. In this work, we applied measures of dynamic variance, like the Gini coefficients, Kullback-Leibler (KL) divergence and dynamic cross correlation (DCC) coefficients to compare the behavior of 3 pairs of homologous proteins from the thermophilic bacterium Thermus thermophilus and mesophilic Escherichia coli. Molecular dynamic (MD) simulations of these proteins were performed at 303 K and 363 K. In the characterization of their side chain rotamer distributions, the corresponding Gini coefficients and KL-divergence both revealed significant correlations with temperature. Similarly, a DCC analysis revealed a higher trend to de-correlate the movement of charged residues at higher temperatures in the thermophilic proteins, when compared with their mesophilic homologues. These results highlight the importance of dynamic electrostatic network interactions for the thermostability of enzymes. (AU) | |
| Processo FAPESP: | 11/50963-4 - Biologia estrutural de proteinas processadoras de acidos nucleicos em bacterias com elevada relevancia biomedica |
| Beneficiário: | Martin Rodrigo Alejandro Wurtele Alfonso |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |