BCH2011 Lecture Notes - Lecture 8: Anfinsen'S Dogma, Pancreatic Ribonuclease, Ribonuclease
Document Summary
A native protein conformation is only marginally stable. In addition, most proteins must maintain conformational flexibility to function. The continual maintenance of the active set of cellular proteins required under a given set of conditions is called proteostasis. Cellular proteostasis requires the coordinated function of pathways for protein synthesis and folding, the refolding of proteins that are partially folded, and the sequestration and degradation of proteins that have been irreversibly unfolded. The marginal stability of most proteins can produce a tenuous balance between folded and unfolded states. As proteins are synthesized on ribosomes, they must fold into their native conformations. Sometimes this occurs spontaneously, but more often it occurs with the assistance of specialized enzymes and complexes called chaperones. Many of these same folding helpers function to refold proteins that become transiently unfolded. Proteins that are not properly folded often have exposed hydrophobic surfaces that render them sticky", leading to the formation of inactive aggregates.
