MBB 222 Study Guide - Midterm Guide: Conformational Entropy, Protein Folding, Thermodynamics
20 Dec 2018
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Protein folding is usually thermodynamically favorable - g for folding is negative due to a balance of several thermodynamic factors: Conformational entropy ( s): works against folding, since the unfolded protein randomly cycles between many possible states (less limited number of conformations) it has a higher entropy value (is more disordered) than the single folded (more ordered) state - Enthalpy contribution ( h): works in favor of folding - formation of energetically favorable interactions - salt bridges, h-bonds, van der waals - between chemical groups in the folded state - h is negative, h<0. Understand the role of chaperones as folding assistants for some proteins. Know the difference between protein domains, globular and fibrous proteins, tertiary and quaternary structure. Many globular proteins consist of several compact, locally folded and stable regions called domains. Domains are often associated with a particular function. Domains tend to have ~40 to 200-350 amino acids. Fewer than 40 amino acids - difficult to fold stably.
