Protein Folding Kinetics

摘要: Publisher Summary This chapter discusses the protein folding kinetics. Protein is often described in terms of a two-state mass-action model, D↔N, where D and N are denatured (or unfolded, U) native folded, F) states, respectively. In folding, there no single microscopic reaction coordinate that every chain follows, may not be identifiable barriers traditional type because energy landscapes funnel shaped. The mechanism has been addressed with mutational studies rates equilibrium constants. methodology, developed as fraction difference (Φ)-value analysis, widely applied to many different proteins. experiments on engineering Φ-value analysis also provide information about transition state structures at level individual residues. A set mutants, strategically distributed over molecule, used map out structure resolution amino acid approach analogously proteins, more complicated contain intermediates pathway, proteins have residual their unfolded states. experimentally determined Φ-values upon substitutions predict critical residues folding. high form nuclei structures, which interactions for rapid assembly