It is observed that as temperature is increased, most protein molecules gofrom their defined, folded state into a random-coil, denatured state thatexposes more hydrophobic surface area than is exposed in the folded state.(a) Given what you have learned so far about ΔH and ΔS, explain why thisis reasonable. (b) Sometimes, however, proteins denature as temperature is decreased.How might this be explained?

The polarity of the solvent and other environmental factors can affect the pKa of a weak acid. Suppose the terminal amino group of a protein has a pKa of about 8.0 when it is exposed to H2O on the outside of a protein.Would you expect the pKa to be higher or lower than 8 if the group were buried in the hydrophobic interior of the protein? Explain

Proteins that are synthesized by living organisms adopt abiologically active conformation. Yet when such moleculesare prepared in the laboratory, they usually fail to spontaneously adopt their active conformations. Can you suggestwhy?

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