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

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 protona...

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Main Author:	Lilia Anghel
Format:	Article
Language:	English
Published:	Academy of Sciences of Moldova, Institute of Chemistry 2015-06-01
Series:	Chemistry Journal of Moldova: General, Industrial and Ecological Chemistry
Subjects:	lactoferrin ionizable residues protonation continuum electrostatics.
Online Access:	http://www.cjm.asm.md/sites/default/files/article_files/ChemJMold201510(1)_71-75_Anghel.pdf

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spelling	doaj-23655956c20a46b48158834f2b4dea4c2021-07-02T03:44:27ZengAcademy of Sciences of Moldova, Institute of ChemistryChemistry Journal of Moldova: General, Industrial and Ecological Chemistry1857-17272345-16882015-06-011017175AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEINLilia Anghel0Institute of Chemistry of the Academy of Sciences of MoldovaIn 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.http://www.cjm.asm.md/sites/default/files/article_files/ChemJMold201510(1)_71-75_Anghel.pdflactoferrinionizable residuesprotonationcontinuum electrostatics.
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Lilia Anghel
spellingShingle	Lilia Anghel AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEIN Chemistry Journal of Moldova: General, Industrial and Ecological Chemistry lactoferrin ionizable residues protonation continuum electrostatics.
author_facet	Lilia Anghel
author_sort	Lilia Anghel
title	AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEIN
title_short	AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEIN
title_full	AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEIN
title_fullStr	AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEIN
title_full_unstemmed	AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEIN
title_sort	investigation of the protonation states of human lactoferrin iron-binding protein
publisher	Academy of Sciences of Moldova, Institute of Chemistry
series	Chemistry Journal of Moldova: General, Industrial and Ecological Chemistry
issn	1857-1727 2345-1688
publishDate	2015-06-01
description	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.
topic	lactoferrin ionizable residues protonation continuum electrostatics.
url	http://www.cjm.asm.md/sites/default/files/article_files/ChemJMold201510(1)_71-75_Anghel.pdf
work_keys_str_mv	AT liliaanghel aninvestigationoftheprotonationstatesofhumanlactoferrinironbindingprotein AT liliaanghel investigationoftheprotonationstatesofhumanlactoferrinironbindingprotein
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AN INVESTIGATION OF THE PROTONATION STATES OF HUMAN LACTOFERRIN IRON-BINDING PROTEIN

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