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Single tryptophan Y160W mutant of homooligomeric E. coli purine nucleoside phosphorylase implies that dimers forming the hexamer are functionally not equivalent

E. coli purine nucleoside phosphorylase is a homohexamer, which structure, in the apo form, can be described as a trimer of dimers. Earlier studies suggested that ligand binding and kinetic properties are well described by two binding constants and two sets of kinetic constants. However, most of the...

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Detalhes bibliográficos
Publicado no:Sci Rep
Main Authors: Narczyk, Marta, Mioduszewski, Łukasz, Oksiejuk, Aleksandra, Winiewska-Szajewska, Maria, Wielgus-Kutrowska, Beata, Gojdź, Adrian, Cieśla, Joanna, Bzowska, Agnieszka
Formato: Artigo
Idioma:Inglês
Publicado em: Nature Publishing Group UK 2021
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC8160210/
https://ncbi.nlm.nih.gov/pubmed/34045551
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-021-90472-4
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