On Bilayer Deformation Energetics With and Without Gramicidin A Channel
Issue Date
2017-08-31Author
Beaven, Andrew H.
Publisher
University of Kansas
Format
155 pages
Type
Dissertation
Degree Level
Ph.D.
Discipline
Chemistry
Rights
Copyright held by the author.
Metadata
Show full item recordAbstract
Lipid membranes are not simply passive barriers. Embedded proteins are coupled to the membrane and can deform the surrounding bilayer, which incurs an energetic penalty. To minimize these penalties, proteins are known to tilt, aggregate, and experience major conformation changes. The degree to which the protein is influenced by the bilayer is dependent on the bilayer material properties and protein-bilayer coupling strength, for example. In this dissertation, the effects of bilayer material properties and protein-bilayer coupling are detailed using gramicidin A channel. This simple channel experiences one major conformational change, its transmembrane dimerization, which produces a bilayer deformation if the bilayer and dimer do not have the same hydrophobic lengths. Herein, molecular dynamics simulations are used to describe bilayer material properties, channel-bilayer coupling, and general lipid energetics with and without gramicidin A.
Collections
- Chemistry Dissertations and Theses [335]
- Dissertations [4701]
Items in KU ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
We want to hear from you! Please share your stories about how Open Access to this item benefits YOU.