On the role of conformational dynamics in enzyme function
2013-12
Loading...
View/Download File
Persistent link to this item
Statistics
View StatisticsJournal Title
Journal ISSN
Volume Title
Title
On the role of conformational dynamics in enzyme function
Authors
Published Date
2013-12
Publisher
Type
Thesis or Dissertation
Abstract
The inherent flexibility of biological macromolecules plays a critical role in their function. This is especially true in the case of enzymes, as these proteins must be able to alter their molecular structures in order to recognize substrates and release products. While they have been shown to be critical for understanding how enzymes function, the exact roles of these structural dynamics are still largely unknown. I have used Nuclear Magnetic Resonance (NMR) Spectroscopy to study the impact of these structural fluctuations for enzyme function in two dramatically different systems: RNA Ligase 10C, a novel enzyme derived via in vitro selection, and the ubiquitous eukaryotic signaling enzyme cAMP-dependent Protein Kinase A (PKA). Despite the variation in their structures and function, I have nonetheless been able to demonstrate the importance of the conformational dynamics of structural elements involved in both systems, suggesting that this is a universal phenomenon, essential for function in all enzymes.
Keywords
Description
University of Minnesota Ph.D. dissertation. December 2013. Major: Biochemistry, Molecular Bio, and Biophysics. Advisors: Gianluigi Veglia, Burckhard Seelig. 1 computer file (PDF); viii, 173 pages.
Related to
Replaces
License
Collections
Series/Report Number
Funding information
Isbn identifier
Doi identifier
Previously Published Citation
Suggested citation
Chao, Fa-An. (2013). On the role of conformational dynamics in enzyme function. Retrieved from the University Digital Conservancy, https://hdl.handle.net/11299/178968.
Content distributed via the University Digital Conservancy may be subject to additional license and use restrictions applied by the depositor. By using these files, users agree to the Terms of Use. Materials in the UDC may contain content that is disturbing and/or harmful. For more information, please see our statement on harmful content in digital repositories.