Learning Goals/Objectives for Chapter 2D:  After class and this reading, students will be able to

• differentiate between thermodynamic (equilibrium) and kinetic (timed) approaches to the study of protein folding reactions
• describe techniques to study transient (kinetic) and long-lived (thermodynamic) intermediates in protein folding
• describe the following intermediates in protein folding:  molten globule, X-Pro isomers; Disulfide bond intermediates
• interpret spectral and chromatographic data from protein folding studies and use this to determine or explain a mechanism for folding
• describe properties of folded, unfolded, molten globule, and intrinsically disordered proteins
• explain the difference between the environments for protein folding when performed in vitro and in vivo
• state the role of molecular chaperones in in vivo protein folding
• describe differences in disulfide bond occurrence in cytoplasmic and extracellular proteins