Work

Observation of strange kinetics in protein folding

Year: 1999

Type: article

Abstract: Highly nonexponential folding kinetics in aqueous solution have been observed during temperature jump-induced refolding of two proteins, yeast phosphoglycerate kinase and a ubiquitin mutant. The observations are most easily interpreted in terms of downhill folding, which posits a heterogeneous ensemble of structures en route to the folded state. The data are also reconciled with exponential kinetics measured under different experimental conditions and with titration experiments indicating cooperative folding.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.96.11.6031

Authors: J. Sabelko, J. Ervin, M. Gruebele

Institutions: University of Illinois Urbana-Champaign, University of Illinois System

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Award: SUBMILLISECOND LASER T JUMP INDUCED PROTEIN FOLDING