Chapter 2
An Introduction to Medicinal Chemistry · 7 exercises
Problem 1
Draw the full structure of L-alanyl-L-phenylalanyl-glycine.
6 step solution
Problem 2
What is unique about glycine compared with other naturally-occurring amino acids?
4 step solution
Problem 3
Identify the intermolecular/intramolecular interactions that are possible for the side chains of the following amino acids; serine, phenylalanine, glycine, lysine, aspartic acid, and aspartate.
6 step solution
Problem 4
The chains of several cell membrane-bound proteins wind back and forth through the cell membrane, such that some parts of the protein structure are extracellular, some parts are intracellular, and some parts lie within the cell membrane. How might the primary structure of a protein help in distinguishing the portions of the protein embedded within the cell membrane from those that are not?
5 step solution
Problem 5
What problems might you foresee if you tried to synthesize L-alanyl-L-valine directly from its two component amino acids?
5 step solution
Problem 6
The tertiary structure of many enzymes is significantly altered by the phosphorylation of serine, threonine, or tyrosine residues. Identify the functional groups that are involved in these phosphorylations and suggest why phosphorylation affects tertiary structure.
4 step solution
Problem 7
What is the one-letter code for the polypeptide Glu-LeuPro-Asp-Val-Val-Ala- Phe-Lys-Ser-Gly-Gly-Thr?
4 step solution