Question

1. The figure below shows the physical representation of a native protein versus a denatured protein 72 native state A-state 23 17 34 72 39 39 34 23 17 (Retrieved from Vajpai, N., Nisius, L., Wiktor, M., & Grzesiek, S. (2013). High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin. Proceedings of the National Academy of Sciences, 110(5), E368-E376.)

a) What aspects of protein structure and folding are explained by entropy? How does entropy
affect a protein’s native versus denatured structure?

b) What aspects of protein structure and folding are explained by enthalpy? How does enthalpy
affect a protein’s native versus denatured structure?

c) What aspects of protein structure and folding are illustrative of equilibrium (or disequilibrium)?

Answer 1

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