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- W2950357632 abstract "Highly conserved throughout the species, homologous recombination is crucial to the survival of any living organism. In humans, the hRad51 protein (human Rad51) plays a key role by self-assembling at the break site on the single stranded extremities of damaged DNA molecules thus forming the nucleoprotein filament. This filament is able by itself to accomplish most of the necessary operations of homologous recombination; it allows the homology search, the pairing of the homologous sequences and the strand exchange.Homologous recombination is a complex process involving many partners. In order to better understand the role of the nucleoprotein filament in this process, we propose to study it in the absence of any partners. We will focus on the study of the mechanical properties of hRad51-dsDNA filaments as a function of chemical conditions. The formation of the nucleoprotein filament modifies the conformation of the DNA molecule on which it assembles, stretching it by 50% and unwinding it by 43% in the case of a double stranded DNA. The magnetic tweezers are a tool allowing the control of the force and torsion applied to a single dsDNA molecule; they are therefore the ideal tool to probe the mechanical properties of nucleoprotein filaments. We modified the magnetic tweezers as to allow the measurement of previously inaccessible mechanical parameters such as the torque applied or felt by the filament. The goal of this thesis has been to study the mechano-chemical properties of nucleoprotein filaments while drawing the energy landscape that governs the various transitions of these systems." @default.
- W2950357632 created "2019-06-27" @default.
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- W2950357632 date "2014-09-26" @default.
- W2950357632 modified "2023-09-27" @default.
- W2950357632 title "Force and torque in magnetic tweezers : energy landscape of the protein hRad51 on double-stranded DNA" @default.
- W2950357632 hasPublicationYear "2014" @default.
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