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Studium interakce membránových proteinů na molekulární úrovni pomocí silové spektroskopie, optické spektroskopie a metod výpočetní biochemie / Membrane protein interactions studied on single molecular level by force spectroscopy, optical spectroscopy and methods of computational biochemistry

I have set for a challenging study that combined experimental and theoretical approaches in an attempt to resolve a role of small aminoacids in intermolecular interactions. First, I have proposed a hypothesis that described the interaction among individual aminoacids forming D helices of D1 and D2 proteins based on molecular dynamic simulations of a simplified model representing the reaction centre of photosystem II. Stability of the putative interhelical hydrogen bond network connecting D1 and D2 proteins was investigated experimentally with dynamic force spectroscopy using atomic force microscope. The results of both methods are in a full agreement with each other and reveal the key role of D1-Gly208 aminoacid in stability and functionality of photosystem II by providing milieu for weak interactions among three contact points at the cross of D helices: D1-Gly208 (O) and D2-Cys211 (O?), D1-Ser209 (O?) and D2-Ile204 (O), D1-Ser212 (O?) and D2-Gly207 (O). Mutation of the D1-Gly208 led to the increase in probability of the binding among the aforementioned aminoacids, undesirably strengthening the overall interactions among the proteins compromising photosynthetic capacity (D1-Ser208) or disabling of autotrophic growth (D1-Val208).

Identiferoai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:85727
Date January 2011
CreatorsMATĚNOVÁ, Martina
Source SetsCzech ETDs
LanguageCzech
Detected LanguageEnglish
Typeinfo:eu-repo/semantics/masterThesis
Rightsinfo:eu-repo/semantics/restrictedAccess

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