Mrs. Carlson Case Study

Keliane Teufack

Mrs Carlson

Questions: 1. What type(s) of bonding is(are) involved at each of the following levels of protein structure (4pts.):

a. Primary – Chain of Amino Acids connected by covalent peptide bond

b. Secondary – Alpha helix and Beta pleated sheet and are connected by a hydrogen bond

c. Tertiary – Create three dimensional where in between there is a hydrophobic interaction, ionic bond, and covalent bond

d. Quaternary – Has the same bonds as tertiary level but it also has interaction between separated polypeptides

The case study background focuses on a specific sulfhydryl group-containing amino acid found in keratin, the principle structural protein in hair.

a. Which amino acid contains a sulfhydryl R-group? -½ pt - Cysteine

b. How do these R-groups interact to contribute to protein structure? -1 pt. - They form ionic bonds, hydrogen bonds, hydrophobic forces, and disulphide bridges between thiol groups on pairs of the Amino Acid cysteine these all help to form a tertiary structure.

c. At which level of protein structure are they used? - ½ pt – They are used at the tertiary level

These amino acids (from Question 2 – containing sulfhydryl groups) are present in many proteins, such as keratin and insulin. Discuss the significance of the loss of this particular amino acid (resulting from a genetic mutation) in the human protein insulin. Address the following questions: (Hint: You may need to find other resources to answer this question.

a. What is the function of the hormone insulin? (1 pt.) - Insulin regulates how the body uses and stores glucose and fat. Which is then used for energy

b. What structural changes may occur to insulin as a result of the mutation resulting in the loss of the sulfhydryl-group-containing amino acid? Why? – 2 pts. - It would result in a total loss of it's 3-D structure because insulin consists of two polypeptide chains, A- and B- linked together by disulfide bonds.

c. In regard to the...