Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.730700
Title: Single-molecule studies of nucleic acid folding and nucleic acid-protein interactions
Author: Pérez González, Daniel Cibrán
ISNI:       0000 0004 6498 8783
Awarding Body: University of St Andrews
Current Institution: University of St Andrews
Date of Award: 2017
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Abstract:
Nucleic acids and proteins, some of the building blocks of life, are not static structures but highly dynamic entities that need to interact with one another to meet cellular demands. The work presented in this thesis focuses on the application of highly sensitive fluorescence methods, both at ensemble and single-molecule level, to determine the dynamics and structure of specific biomolecular interactions with nanometer resolution and in temporal scales from nanoseconds to minutes, which includes most biologically relevant processes. The main aims of my PhD can be classified in three areas: i) exploring new fluorescent sensors with increased specificity for certain nucleic acid structures; ii) understanding how some of these nucleic acids sense the presence of small molecules in the cellular environment and trigger gene regulation by altering their structure; and iii) understanding how certain molecular machines, such as helicase proteins, are able to unwind the DNA double helix by using chemical energy in the form of ATP hydrolysis.
Supervisor: Penedo Esteiro, Juan Carlos Sponsor: Engineering and Physical Sciences Research Council (EPSRC) ; University of St Andrews
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.730700  DOI: Not available
Keywords: RNA folding ; Riboswitch ; TIRF microscopy ; Fluorescence resonance energy transfer (FRET) ; G-quadruplex ; Helicase unwinding ; QP620.P474 ; Nucleic acids--Analysis ; Proteins ; DNA-protein interactions ; RNA-protein interactions
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