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KIVO Med

Amino acids: structure, properties, and study methods

From the units of proteins to their reactions and analytical separation, this course establishes the framework needed to reason about amino acids.

  • 75 explained questions
  • 23 flashcards
  • 172 estimated course minutes

Updated

What you will learn

  • Describe the general structure of an α-amino acid and its exceptions.
  • Classify amino acids by their side chain, polarity, origin, and metabolic fate.
  • Relate chirality, charge, isoelectric point, solubility, and light absorption to study methods.
  • Identify the main reactions of carboxyl, amino, and side-chain groups.

Course outline

  1. Building blocks of proteins

    Connect amino acids with protein diversity, food supply, and metabolic pathways.

    10 min

  2. Structure, repertoire, and coding

    Recognise the α-amino-acid scaffold, distinguish different AA repertoires, and read their symbols in a sequence.

    28 min

  3. Classifying by side chain, origin, and fate

    Learn three complementary classifications without confusing them: side-chain properties, dietary requirement, and carbon-skeleton fate.

    34 min

  4. Chirality, charge, spectrum, and solubility

    Relate alpha-carbon geometry, ionisation, and side-chain nature in turn to measurable amino-acid properties.

    38 min

  5. Reacting carboxyl, amino, and R groups

    Distinguish reactions carried by COOH, NH2, and side chain R, then link each reaction to its use.

    28 min

  6. Separating and identifying amino acids

    Choose a method from the molecular property that it turns into migration, a band, or a retention time.

    34 min

Study and practise with KIVO Med

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Educational resources for medical studies; they do not replace your faculty’s teaching or medical advice.

In the same subject

  • Peptides: bonds, properties and analysis

    Build, represent and analyse a peptide, from its amide bond to its biological roles.

  • Proteins

    From amino-acid sequence to purification and sequencing, linking protein structure to physicochemical properties and function.

  • Amino-acid metabolism

    Follow amino-acid nitrogen and carbon skeletons through catabolism, synthesis, and representative aminoacidopathies.