BIO 2133 Chapter Notes - Chapter 14.9-14.12: Proteasome, Peptide, Carbohydrate
Document Summary
14. 9 variation in protein structure provides the basis of biological diversity. Proteins perform and control cellular activities in an organism are precursors of proteins amino acid polymer is assembled, folded up, The 3d shape is essential, determines the functionality. Types of amino acids: nonpolar, polar, positively charged, negatively charged. Peptide bonding of amino acids = amino group + carboxyl group (dehydration reaction) Primary = sequence of amino acids, linear backbone. Secondary = configurations in space of amino acids lying close to one another e. g. alpha helix, beta pleated sheet, etc. Tertiary = 3d spatial conformation of the chain as a whole, polypeptides twist and turn covalent disulfide bonds, and hydrophobic/philic groups determine the conformation. Quaternary = only applies to proteins composed of more than one polypeptide chain refers to the position of the various chains in relation to one another. ** lists of all the amino acids can be found online, with their various characteristics **