Millisecond and Submillisecond Folding Kinetics of Horse Apomyoglobin and Yeast Phosphoglycerate Kinase
Sabelko, Jobiah John
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https://hdl.handle.net/2142/84496
Description
Title
Millisecond and Submillisecond Folding Kinetics of Horse Apomyoglobin and Yeast Phosphoglycerate Kinase
Author(s)
Sabelko, Jobiah John
Issue Date
2000
Doctoral Committee Chair(s)
Martin Gruebele
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
Yeast 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).
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