AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEIN

Autor:	Lilia Anghel
Jazyk:	angličtina
Rok vydání:	2015
Předmět:	lactoferrin ionizable residues protonation continuum electrostatics. Chemistry QD1-999 General. Including alchemy QD1-65
Zdroj:	Chemistry Journal of Moldova: General, Industrial and Ecological Chemistry, Vol 10, Iss 1, Pp 71-75 (2015)
Druh dokumentu:	article
ISSN:	1857-1727 2345-1688
Popis:	In this study, the protonation states of ionizable groups of human lactoferrin in various conformations were investigated theoretically, at physiological pH (7.365). These calculations show that the transition of the protein from a conformation to another one is accompanied by changes in the protonation state of specific amino acid residues. Analysis of the pKa calculatons underlined the importance of participation of two arginines and one lysine in the opening / closing of the protein. In addition, it was found that the mechanism of iron release depends on the protonation state of TYR-192. Protonated state of this residue in the closed form of lactoferrin will trigger the opening of protein and release of iron ions.
Databáze:	Directory of Open Access Journals
Externí odkaz:	https://doaj.org/article/23655956c20a46b48158834f2b4dea4c Zobrazit plný text záznamu View record in DOAJ