Carregant...
Fitxers
Tipus de document
ArticleVersió
Versió publicadaData de publicació
Llicència de publicació
Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/172314
Effect of pH on the supramolecular structure of helicobacter pylori urease by molecular dynamics simulations
Títol de la revista
Director/Tutor
ISSN de la revista
Títol del volum
Recurs relacionat
Resum
The effect of pH on the supramolecular structure of Helicobacter pylori urease was studied by means of molecular dynamics simulations at seven different pHs. Appropriate urease charge distributions were calculated using a semi-grand canonical Monte Carlo (SGCMC) procedure that assigns each residue's charge state depending on the assigned individual pKa obtained by PROPKA. The effect of pH on protein stability has been analyzed through root-mean-square deviation (RMSD), radius of gyration (RG), solvent-accessible surface area (SASA), hydrogen bonds (HB) and salt bridges (SB). Urease catalyses the hydrolysis of urea in 12 active sites that are covered by mobile regions that act like flaps. The mobility of these flaps is increased at acidic pHs. However, extreme acidic conditions cause urease to have the least number of stabilizing interactions. This initiates the process of denaturalization, wherein the four (αβ)3 subunits of the global structure ((αβ)3)4 of urease start to separate.
Matèries (anglès)
Citació
Citació
BARAZORDA-CCAHUANA, Haruna l., GÓMEZ, Badhin, MAS I PUJADAS, Francesc, MADURGA DÍEZ, Sergio. Effect of pH on the supramolecular structure of helicobacter pylori urease by molecular dynamics simulations. _Polymers_. 2020. Vol. 12, núm. 11, pàgs. 2713. [consulta: 22 de desembre de 2025]. ISSN: 2073-4360. [Disponible a: https://hdl.handle.net/2445/172314]