Proteins
Proteins
This lesson develops Proteins as part of Gene Expression. It uses the source curriculum to organize the important facts, relationships, examples, and vocabulary into a focused Stemosphere teaching sequence.
Keep the central model in view: Proteins explains observable patterns by connecting structure, process, evidence, and quantitative relationships.
In Stemosphere terms, general Structure of Amino Acids
All amino acids share a common framework:
In Stemosphere terms, central (α) Carbon– the core atom of the amino acid.
In Stemosphere terms, hydrogen Atom (H)– attached to the α-carbon.
In Stemosphere terms, amino Group (–NH₂)– acts as a base.
In Stemosphere terms, carboxyl Group (–COOH)– acts as an acid.
Apeptide bondforms between:
In Stemosphere terms, thecarboxyl group (–COOH)of one amino acid
In Stemosphere terms, during the reaction,–OHfrom the carboxyl group and–Hfrom the amino group are removed.
In Stemosphere terms, this produceswater (H₂O).
In Stemosphere terms, primary Protein Structure
In Stemosphere terms, it is determined by thenucleotide sequence of a gene.
In Stemosphere terms, amino acids are linked bypeptide bondsformed throughcondensation reaction s.
In Stemosphere terms, proteins fold into precise, predictable shapesbased on their amino acid sequence.
In Stemosphere terms, secondary Protein Structure
Thesecondary structureis thefolding of a polypeptideinto:
Folding occurs due tohydrogen bondsbetween:
The C=O group of one amino acidIn Stemosphere terms, tertiary Protein Structure
In Stemosphere terms, ionic bonds– form between charged R group s(e.g., amine and carboxyl group s that gain or lose H⁺).
In Stemosphere terms, covalent bonds– includedisulfide bridgesbetweencysteine R group s(–S–S–).
In Stemosphere terms, hydrogen bonds– between polar R group s.
In Stemosphere terms, disulfide Bonds (Bridges)
In Stemosphere terms, form between two cysteine amino acidsin close proximity.
In Stemosphere terms, covalent bond forms between thesulfur atomsof their R group s, stabilizing the protein’s 3D shape.
In Stemosphere terms, quaternary Protein Structure
In Stemosphere terms, found in proteins composed ofmore than one polypeptide chain.
In Stemosphere terms, stabilizing Interactions Between Polypeptides
In Stemosphere terms, covalent bonds(e.g., disulfide bridges)
In Stemosphere terms, the quaternary structure allows proteins toform complex, functional 3D shapesnecessary for biological activity.
Example
Haemoglobin
In Stemosphere terms, globular conjugated protein
Composed of:
2 alpha polypeptide chains
2 beta polypeptide chains
4 haem group s(non-polypeptide prosthetic group s)
In Stemosphere terms, proteinscomposed only of polypeptides(no prosthetic group).
In Stemosphere terms, globular protein with2 polypeptide chainslinked by2 disulfide bridges
In Stemosphere terms, fibrous protein with3 polypeptide chainscoiled into atriple helix
In Stemosphere terms, classification Based on Shape
In Stemosphere terms, insulin:Globular protein (spherical, functional)
In Stemosphere terms, both aremade of amino acids joined by peptide bondsduring translation on ribosomes.
In Stemosphere terms, irregular amino acid sequence with hydrophobic amino acids in the core
In Stemosphere terms, composed of2 polypeptide chainslinked by disulfide bonds
In Stemosphere terms, functional protein (hormone) that binds to receptors on target cells and is transported in the blood
In Stemosphere terms, repetitive amino acid sequence