Proteins have a high thermodynamic instability. Despite the fact that the G of protein hydrolysis is fairly negative, proteins may be quite stable. Explain the seeming contradiction. What does this mean in terms of protein synthesis?

Which of the following statements are correct about the thermodynamics of protein folding (select all that appy)?   A. The deltaG for protein folding is negative   B. Burial of hydrophobic side provides a positive entropy change that drive protein folding   C. The overall entropy change of protein folding is favorable   D. Intercations between amino acids provide a large negative deltaH that helps favor the native state.   E. The free energy change of protein folding is dependent on the temperature

This image is showing the conformations of ubiquitin superimposed. What do the structures in this figure tell us about the dynamics of enzymes? Discuss the limitations of crystal structures in the analysis of proteins. What are the benefits? What are the advantages of NMR structures?

A cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.