Structure of a kinetic protein folding intermediate by equilibrium amide exchange.
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.
Hosszu
L L
LL
Craven
C J
CJ
Parker
M J
MJ
Lorch
M
M
Spencer
J
J
Clarke
A R
AR
Waltho
J P
JP
D000577:Amides; D004795:Enzyme Stability; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D006358:Hot Temperature; D006860:Hydrogen Bonding; D007700:Kinetics; D008958:Models, Molecular; D008962:Models, Theoretical; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D000577:Amides; D010735:Phosphoglycerate Kinase