Effects of Domain Dissection on the Folding and Stability of the 43 kDa Protein PGK Probed by NMR

The characterization of early folding intermediates is key to understanding the protein folding process. Previous studies of the N-domain of phosphoglycerate kinase (PGK) from Bacillus stearothermophilus combined equilibrium amide exchange data with a kinetic model derived from stopped-flow kinetics...

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Veröffentlicht in:	Journal of molecular biology 2003-07, Vol.330 (5), p.1189-1201
Hauptverfasser:	Reed, Michelle A.C., Hounslow, Andrea M., Sze, K.H., Barsukov, Igor G., Hosszu, Laszlo L.P., Clarke, Anthony R., Craven, C.Jeremy, Waltho, Jonathan P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Algorithms assignment Bacillus stearothermophilus Computer Simulation folding Geobacillus stearothermophilus - enzymology Hydrogen Bonding kinetic intermediate Kinetics Magnetic Resonance Spectroscopy Monte Carlo Method NMR phosphoglycerate kinase Phosphoglycerate Kinase - chemistry Protein Binding Protein Folding Protein Structure, Tertiary
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