Consider two proteins, Protein A and Protein B: A is a monomeric protein, whereas B is a subunit of a homo-tetrameric protein. Both A and B are soluble. Additionally, both A and B have similar 3D structures. What differences would you expect to see between the amino acids exposed on the surfaces of A and B? Explain the reasons for the differences observed.

Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bonds

Consider protein folding that results when the following components interact:   Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.

HOW MANY DIFFERENT PROTEINS CAN BE CONSTRUCTED THAT ARE EXACTLY FOUR AMINO ACIDS LONG? (HINT: THERE ARE 20 POSSIBLE AMINO ACIDS.)