CHEM 451 Lecture Notes - Lecture 8: Protein Folding, Energy Landscape, Protein Structure
Document Summary
Measure kinetics in folding and unfolding protein by changing conditions of protein (eg. rapid exchange from buffer to chemical denaturant and follow kinetic response of protein from being in that solution) Some amplitude change, increase or decrease depending on folding or unfolding depending on time. In exponent = k observe (gets plotted in the chart below) k obvs ??????? kobvs = kf + ku. Each point represents a curve, start in water and dilute in denaturant (giving unfolding arm) vs start in denaturant then move to water or buffer (gives folding arm) Extrapolation of arms give folding and unfolding rate. Can determine folding and folding rate, k obvs is what we determine. If close to 1 -> mutant is structured in. Phi value is indirect way to find what is present in transition state. Reengineer folding pathway, want to show that they have changed what is present in the transition state in the reengineered protein.
