Structure of a kinetic protein folding intermediate by equilibrium amide exchange

L L Hosszu; C J Craven; M J Parker; M Lorch; J Spencer; A R Clarke; J P Waltho

doi:10.1038/nsb1097-801

Structure of a kinetic protein folding intermediate by equilibrium amide exchange

Nat Struct Biol. 1997 Oct;4(10):801-4. doi: 10.1038/nsb1097-801.

Authors

L L Hosszu, C J Craven, M J Parker, M Lorch, J Spencer, A R Clarke, J P Waltho

PMID: 9334744
DOI: 10.1038/nsb1097-801

Abstract

A combination of equilibrium amide exchange and kinetic folding data show that the essential features of the complex topology of the N-terminal domain of a thermophilic phosphoglycerate kinase are established on a millisecond or faster timescale, before the rate-limiting step in the folding pathway commences.

Publication types

Letter
Research Support, Non-U.S. Gov't

MeSH terms

Amides
Enzyme Stability
Geobacillus stearothermophilus / enzymology
Hot Temperature
Hydrogen Bonding
Kinetics
Models, Molecular
Models, Theoretical
Phosphoglycerate Kinase / chemistry*
Phosphoglycerate Kinase / metabolism*
Protein Folding*
Protein Structure, Secondary*
Thermodynamics

Substances

Amides
Phosphoglycerate Kinase