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Stability of the dimeric and hexameric form of purine nucleoside phosphorylase from Escherichia coli – a computational study (CROSBI ID 374228)

Ocjenski rad | diplomski rad

Hajnić, Matea Stability of the dimeric and hexameric form of purine nucleoside phosphorylase from Escherichia coli – a computational study / Bertoša, Branimir (mentor); Zagreb, Prirodoslovno-matematički fakultet, Zagreb, . 2012

Podaci o odgovornosti

Hajnić, Matea

Bertoša, Branimir

engleski

Stability of the dimeric and hexameric form of purine nucleoside phosphorylase from Escherichia coli – a computational study

Purine nucleoside phosphorylase (PNP) is one of the key enzymes in purine salvage pathway which helps cells to recover nucleotides from degradation intermediates of nucleic acids. Biologically active form of PNP in Escherichia coli is a homohexamer, also seen as a trimer of dimers mutually connected with non-covalent bonds, and still with no cooperativity proven between them. In order to examine if a dimer is sufficient for catalysis, combinations of mutations were introduced in silico into hexameric structure of wild type PNP from E.coli. Mutations or combinations thereof were introduced to disrupt the homohexameric form and to obtain stable dimers in solution. Based on the results obtained from molecular dynamic simulations, a mutant with the most promising combination of mutations was identified. These specific mutations could potentially cause the breakdown of hexameric structure and result in the formation of stable dimers.

molecular dynamics ; molecular mechanics ; in silico mutations

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Podaci o izdanju

27

24.09.2012.

obranjeno

Podaci o ustanovi koja je dodijelila akademski stupanj

Prirodoslovno-matematički fakultet, Zagreb

Zagreb

Povezanost rada

Biologija, Kemija