Millisecond and Submillisecond Folding Kinetics of Horse Apomyoglobin and Yeast Phosphoglycerate Kinase
type: CreativeWork
description: 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).
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).
author: Sabelko, Jobiah John
language: eng
keywords: Chemistry, Biochemistry
date published: 2015-09-25T22:14:48Z
date modified: 2026-07-22T22:26:23Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/84496