Skip to content

KIVO Med

Peptides: bonds, properties and analysis

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

  • 43 explained questions
  • 33 flashcards
  • 261 estimated course minutes

Updated

What you will learn

  • Describe formation, geometry and polarity of the peptide bond.
  • Represent, name and classify a peptide sequence.
  • Explain peptide properties, hydrolysis and analytical methods.
  • Relate several biological peptides to their described structure and function.

Course outline

  1. From amino acid to peptide message

    Locate the peptide chain, its residues, and its orientation before studying its geometry, properties, and analytical methods.

    12 min

  2. Forming the bond and orienting the chain

    Follow separately the condensation that creates the amide and the preservation of the N- and C-terminal ends.

    19 min

  3. A planar, rigid, polar amide bond

    Infer local peptide geometry from resonance, then distinguish the amide plane, cis–trans, rotation angles, and polarity.

    36 min

  4. Writing, naming, and cyclising a sequence

    Read a chain from N to C, distinguish backbone from side chains, apply nomenclature, and recognise head-to-tail cyclisation.

    20 min

  5. Classifying by size, form, function, and origin

    Apply four classification axes separately and interpret their conventional thresholds cautiously.

    20 min

  6. Solubility, charge, and UV absorption

    Relate size, composition, ionisable groups, and aromatic residues separately to measurable peptide properties.

    21 min

  7. Chemical reactivity and disulphide bridges

    Study esterification, cysteine redox chemistry, colour tests, and hydrolysis as separate reactions.

    26 min

  8. Synthesis, maturation, and enzymatic hydrolysis

    Distinguish ribosomal construction, maturation, non-ribosomal synthesis, and terminal or internal cleavage.

    25 min

  9. Hydrolysing and quantifying amino acids

    Choose a hydrolysis, separate released AAs, then reveal and quantify each constituent.

    24 min

  10. Reconstructing the sequence

    Cross terminal information with specifically cleaved fragments to place residues in order.

    32 min

  11. From peptides to biological functions

    Compare peptides by sequence, disulphide bridges, location, and biological function.

    26 min

Study and practise with KIVO Med

This preview shows the available content. Full courses, explanations and flashcards are available in the app with an account and access to the relevant programme. Prices and access terms are shown there.

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

In the same subject

  • 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.

  • 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.