Amino Acids: Zwitterions, Isoelectric Point and Peptide Bond Formation
Students will be introduced to amino acids as building blocks of proteins and understand the basic concept of protein formation and function.
Key Questions
- Explain the formation of a zwitterion from an amino acid and calculate the isoelectric point from pKa data for the α-amino and α-carboxyl groups, predicting the net charge at physiological pH.
- Construct the mechanism for peptide bond formation via nucleophilic acyl substitution and explain why the peptide bond exhibits partial double-bond character, relating this to restricted rotation and secondary structure consequences.
- Analyse how the R-group polarity and charge state of amino acids at a given pH determines their separation by gel electrophoresis and ion-exchange chromatography.
MOE Syllabus Outcomes
Suggested Methodologies
Ready to teach this topic?
Generate a complete, classroom-ready active learning mission in seconds.
Planning templates for Chemistry
More in Organic Mechanisms: Nucleophilic Substitution, Elimination and Electrophilic Addition
Introduction to Organic Compounds and Hydrocarbons
Students will define organic chemistry, identify common organic compounds, and classify simple hydrocarbons (alkanes, alkenes) based on their bonding.
2 methodologies
Alcohols: Oxidation, Dehydration and Nucleophilic Substitution
Students will identify alcohols as a functional group, describe their general properties, and explore their common uses.
2 methodologies
Carboxylic Acids, Acyl Chlorides and Ester Hydrolysis Mechanisms
Students will identify carboxylic acids and esters, understand their basic properties, and learn about the formation of esters (esterification).
2 methodologies
Polymer Synthesis: Addition and Condensation Mechanisms
Students will learn about polymers as large molecules made from repeating units, focusing on common synthetic polymers (plastics) and their formation.
2 methodologies