Computational Study of MutH Recognition and Catalysis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F09%3A00039550" target="_blank" >RIV/00216224:14310/09:00039550 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Computational Study of MutH Recognition and Catalysis

Popis výsledku v původním jazyce

MutH enzyme participates in methyl-directed DNA repair together with two other enzymes MutS and MutL. Their joint choreography is conceptually known but a lot of details are still elusive. We aim to resolve to two challenging questions related to the recognition and catalytic activity of MutH by utilizing computational techniques. 1) How a single methyl group attached to a far-lying adenine base from the active site can determine the activity of MutH? 2) Is Lys-77 residue serves to couple recognition tocatalysis?

Název v anglickém jazyce

Computational Study of MutH Recognition and Catalysis

Popis výsledku anglicky

MutH enzyme participates in methyl-directed DNA repair together with two other enzymes MutS and MutL. Their joint choreography is conceptually known but a lot of details are still elusive. We aim to resolve to two challenging questions related to the recognition and catalytic activity of MutH by utilizing computational techniques. 1) How a single methyl group attached to a far-lying adenine base from the active site can determine the activity of MutH? 2) Is Lys-77 residue serves to couple recognition tocatalysis?

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2009

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů