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...

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Veröffentlicht in:	Nature Structural Biology 1997-10, Vol.4 (10), p.801-804
Hauptverfasser:	Hosszu, Laszlo L. P, Craven, C. Jeremy, Parker, Martin J, Lorch, Mark, Spencer, James, Clarke, Anthony R, Waltho, Jonathan P
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides Biochemistry Biological Microscopy Biomedical and Life Sciences correspondence Enzyme Stability Geobacillus stearothermophilus - enzymology Hot Temperature Hydrogen Bonding Kinetics Life Sciences Membrane Biology Models, Molecular Models, Theoretical Phosphoglycerate Kinase - chemistry Phosphoglycerate Kinase - metabolism Protein Folding Protein Structure Protein Structure, Secondary Thermodynamics
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Beschreibung
Zusammenfassung:	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.
ISSN:	1072-8368 2331-365X 1545-9985
DOI:	10.1038/nsb1097-801