Protein Folding Notes

Protein Structure = Protein Function In order to perform its specific job in the cell, a protein must fold into its proper shape

Levels of Protein Folding Primary The order of amino acids in a polypeptide chain

Levels of Protein Folding Secondary Folding caused by interactions within the protein’s backbone β pleated sheet α helix

Levels of Protein Folding Tertiary Folding caused by bonding between amino acid R groups Opposites (positive and negative) attract Cysteine covalently bonds with other cysteines Hydrophobic amino acids move to the middle Hydrophilic amino acids move to the outside

Tertiary Structure

Levels of Protein Folding Quaternary Individual polypeptide chains come together to form a multi-subunit protein

Watch Proteins Fold! http://lab.concord.org/embeddable.html#interactives/samples/5- amino-acids.json

To Sum Up

Make a Protein! Positively Charged Negatively Charged Hydrophilic Hydrophobic Histidine Aspartic Acid Serine Methionine Arginine Glutamic Acid Threonine Glycine Lysine   Glutamine Tyrosine Proline Isoleucine Asparagine Leucine Cysteine  Alanine Valine Phenylalanine Tryptophan