University of Illinois at Urbana-Champaign
Millisecond and Submillisecond Folding Kinetics of Horse Apomyoglobin and Yeast Phosphoglycerate Kinase
Abstract
dc:descriptionYeast phosphoglycerate kinase is a 415 residue dual domain protein which contains two tryptophans located in the C-terminus. PGK readily cold denatures yielding a state generally devoid of stable secondary structure. Kinetic measurements indicated the molecule collapses to a molten globule type state on the sub-ms time scale. Measurements on the wild-type protein and a series of single tryptophans mutants also showed vastly different folding times indicating considerable folding heterogeneity both interdomain and intradomain. Furthermore, by varying the final folding temperature and thereby adjusting the native bias, the kinetics were successfully tuned between type 1 (activated) and type 0 (downhill).
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Chemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Sabelko, Jobiah John
- Contributors dc:contributor
-
- Martin Gruebele
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI9990127
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/84496