Theoretical Questions 1. Draw the general structure of the zwitterion form of an amino acid using the letter R for the side chain group. What is the term given for the pH range at which an amino acid exists in the zwitterion form? 2. What functional group results when amino acids are linked together? 3. Give the four different classifications for amino acids. Which ones have side chains that could have a charge? 4. Define Denaturation. Changes in which levels of protein structure could cause denaturation could occur?

Explain why casein precipitates when vinegar is added. Why was milk or raw egg once used as an antidote in cases of heavy metal poisoning? Based on your isolated yield of casein, how many grams of the protein are in one 200 g glass of milk? Which of the solutions contained amide bonds? Which test tells you this? Which of the solutions contained compounds with primary amino groups? Which test tells you this? Describe two examples of protein folding patterns and identify what level of protein structure they belong to. What other reagents might you use besides ferric chloride to test affinity for metal ions?

6. Is this amino acid L- or D-, and how can you tell? Н -ŅH3 CH3 a. D-, because all amino acids are D. b. D-, because the amine is on the right. c. D-, because the amine is on the left. d. L-, because the amine is on the left.

Select all that apply   Select all the statements that correctly describe protein formation. Multiple select question. Proteins are formed between amino acid monomers. Proteins are biological addition polymers. When the carboxy group reacts with the amino group to form the protein, a carbon dioxide molecule is eliminated. Proteins are formed when the amino group of one monomer reacts with a carboxy group of another.

4. Nylon has been called a synthetic structural protein. What organic functional group do nylon and proteins have in common?

Identify each of the amino acids in the structure.

Identify which of the following pairs of amino acid residues can have hydrogen bonding between their side chains.a. Alanine and Glycineb. Leucine and Isoleucinec. Valine and Asparagined. Threonine and Tyrosine2. Draw a picture showing the details of the hydrogen bonding among the pairs in exercise 1