Competitive Interaction of Component Enzymes with the Peripheral Subunit-Binding Domain of the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus stearothermophilus : Kinetic Analysis Using Surface Plasmon Resonance Detection †

Conformational analysis of peptide fragm

Conformational analysis of peptide fragments derived from the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Evidence for nonrandom structure in the unfolded state

✍ Shari Spector; Michael Rosconi; Daniel P. Raleigh 📂 Article 📅 1999 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 195 KB

There is currently a great deal of interest in the early events in protein folding. Two issues that have generated particular interest are the nature of the unfolded state under native conditions and the role of local interactions in folding. Here, we report the results of a study of a set of peptid