Abstract
dc:description.abstractLife is soft. From the fluid-like structure of lipid bilayers to the flexible folding of proteins, the realm of nanoscale soft matter is a complex and vibrant area of research. The lure of personalized medicine, advanced sensing technology, and understanding life at a fundamental level pushes research forward. This work considers to areas: (1) lipid bilayer dynamics in the presence of substrate defects and (2) the inverse temperature transition of elastic proteins. Molecular dynamics simulations as well as umbrella sampling were employed. The behavior of the bilayers discussed in the work provides evidence that small defects on confining surfaces can promote nucleation of lipid tethers. Results the second part of this work indicate elastin-like peptides experiencing inverse temperature transitions may be capable of performing amounts of work similar to RNA polymerase; additionally, resilin's inverse temperature transition may be closely linked to the molecule's ability to efficiently transmit energy through the similar coil-β secondary structure transition seen in both cases. These insights into the inverse transition temperature are relevant for the design of bio-inspired sensors and energy storage devices.
Degree
thesis:*- Name thesis:degree_name
- Master of Science
- Level thesis:degree_level
- masters
- Discipline thesis:degree_discipline
- Engineering Mechanics
- Department dc:contributor.department
- Engineering Science and Mechanics
- Grantor dc:publisher
- Virginia Tech
- Year dc:date.issued
- 2014
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Fergusson, Austin D.
- Chair dc:contributor.committeechair
-
- Holmes, Douglas P.
- Committee members dc:contributor.committeemember
-
- Jung, Sunghwan
- Staples, Anne E.
Subjects
dc:subject × 6Rights
dc:rights- Statement dc:rights
-
- In Copyright
- Licence dc:rights.uri
Identifiers
dc:identifier.*- Dc Identifier Other
- vt_gsexam:3545
- OAI identifier oai:identifier
- oai:vtechworks.lib.vt.edu:10919/50500