Date of Graduation
12-2019
Document Type
Dissertation
Degree Name
Doctor of Philosophy in Chemistry (PhD)
Degree Level
Graduate
Department
Chemistry & Biochemistry
Advisor/Mentor
Heyes, Colin D.
Committee Member
Adams, Paul D.
Second Committee Member
Chen, Jingyi
Third Committee Member
Henry, Ralph L.
Fourth Committee Member
Thallapuranam, Suresh
Keywords
cpSRP; disordered; dynamics; protein; structure; targeting
Abstract
The work presented in this dissertation explores the structural dynamics in the chloroplast signal recognition particle pathway. Findings include cpSRP shows scanning functionality similar to that in the cytosolic SRP with the ribosome. The intrinsically disordered C-terminal tail of the Albino3 protein has some transient secondary structure. Upon binding to cpSRP43 in solution, separate secondary structure formation was identified in the C-terminal tail of Albino3. Finally, to increase efficiency of analyzing fluorescence time traces for this work, a modular software was produced.
Citation
Baucom, D. R. (2019). Single Molecule Fluorescence Studies of protein structure and dynamics underlying the chloroplast signal recognition particle targeting pathway. Graduate Theses and Dissertations Retrieved from https://scholarworks.uark.edu/etd/3465
Included in
Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Biophysics Commons, Molecular Biology Commons, Structural Biology Commons
