2009
Revealing the mysteries of the RS20L lectin from Ralstonia solanacearum ; a molecular modelling study
ĎURECH, Michal, Jan ADAM, Zdeněk KŘÍŽ, Nikola KOSTLÁNOVÁ, Jaroslav KOČA et. al.Základní údaje
Originální název
Revealing the mysteries of the RS20L lectin from Ralstonia solanacearum ; a molecular modelling study
Název česky
Revealing the mysteries of the RS20L lectin from Ralstonia solanacearum ; a molecular modelling study
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Vydání
Brno, XIII. Setkání biochemiků a molekulárních biologů, s. 109-109, 2009
Nakladatel
Masarykova Univerzita
Další údaje
Jazyk
angličtina
Typ výsledku
Stať ve sborníku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Organizační jednotka
Přírodovědecká fakulta
ISBN
978-80-210-4830-0
Klíčová slova česky
lectin engineering; molecular modeling; thermodynamics
Klíčová slova anglicky
lectin engineering; molecular modeling; thermodynamics
Změněno: 9. 4. 2010 09:24, prof. RNDr. Michaela Wimmerová, Ph.D.
V originále
Our research is focused on bacterial lectin RS20L from Ralstonia solanacearum.The RS20L lectin displays a different structure from these two, and no structure homologue was found for this lectin in the bacterial lectin realm. Its fold resembles animal realm galectins. The native lectin structure was crystallized, and during the experimental preparation of a recombinant form and attempts of functional characterization, several cases of very peculiar behavior were recorded extremely high stability of trimeric form, irreversible loss of binding properties after purification, etc. The research focuses on investigating the general and binding properties of the RS20L lectin that could help to explain this unusual behaviour. The study was performed by means of computational chemistry and molecular modelling. Several promising hints were found that could, upon further investigation, help to decrypt the reasons behind the lectin behavior.
Česky
Prace se zabyva lektinem RS20L z bakterie Ralstonia solanacearum. Tento lektin se v rade pripadu chova velmi neobvykle. Metody molekuloveho modelovani aplikovane na tento system napomohly objevit nekolik dalsich informaci, ktere by mohly vysvetlovat vazebne i obecne chovani tohoto proteinu.
Návaznosti
GA303/09/1168, projekt VaV |
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MSM0021622413, záměr |
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