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A comparative study on nickel binding to Hpn-like polypeptides from two Helicobacter pylori strains
Autorzy
Rok wydania
2021
Czasopismo
International Journal of Molecular Sciences
Numer woluminu
22
Strony
13210/1-13210/15
DOI
10.3390/ijms222413210
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
Combined potentiometric titration and isothermal titration calorimetry (ITC) methods were used to study the interactions of nickel(II) ions with the N-terminal fragments and histidine-rich fragments of Hpn-like protein from two Helicobacter pylori strains (11637 and 26695). The ITC measurements were performed at various temperatures and buffers in order to extract proton-independent reaction enthalpies of nickel binding to each of the studied protein fragments. We bring up the problem of ITC results of nickel binding to the Hpn-like protein being not always compatible with those from potentiometry and MS regarding the stoichiometry and affinity. The roles of the ATCUN motif and multiple His and Gln residues in Ni(II) binding are discussed. The results provided the possibility to compare the Ni(II) binding properties between N-terminal and histidine-rich part of Hpn-like protein and between N-terminal parts of two Hpn-like strains, which differ mainly in the number of glutamine residues.
Słowa kluczowe
nickel binding, H. pylori, Hpn-like, histidine-rich, glutamine-rich, ATCUN motif
Licencja otwartego dostępu
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Pełny tekst licencji: https://creativecommons.org/licenses/by/3.0/pl/legalcode
Adres publiczny
http://dx.doi.org/10.3390/ijms222413210
Strona internetowa wydawcy
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