1. What type of reaction links two amino acids into a dipeptide? 2. What functio

ID: 541632 • Letter: 1

Question

1. What type of reaction links two amino acids into a dipeptide?

2. What functional groups are found in the peptide backbone?

3. Would a peptide in solution be vulnerable to cleavage by addition of a strong base to the solution?

4. Where does the R group or side chain connect to the backbone of an amino acid?

5. Are polypeptides linear or branched polymers?

6. Where are hydrophobic side chains generally found in a globular protein?

7. Where are hydrophilic side chains generally found in a globular protein?

8. What non-covalent interaction stabilizes an alpha helix?

9. What non-covalent interaction stabilizes an beta sheet?

10. What is the most important feature of primary structure?

11. What mediates the formation of tertiary structure in a polypeptide or protein?

12. What distinguishes quaternary structure from tertiary structure?

13. What non-covalent interactions are disrupted when a protein is denatured?

14. What amino acid residues participate to form a disulfide bond?

15. Does a protein that exists as a monomer have quaternary structure? Explain your answer, a simple yes or no will receive no credit?

1. condensation reaction formed on losing H2O molecule while combining amine of one amino acid to carboxylic acid of another

2. amides

3. yes liable to cleavage on addition of base

4 attached to the alpha carbon which is specific to amino acid

5. both

6. hydrophobic R-groups buried deep within their core, creating a water excluding region

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