BIO206H5 Lecture Notes - Lecture 4: Glutamine, Asparagine, Isoleucine
Document Summary
Optical isomers (mirror images of each other) Proline (pro) - 5 carbon - p. The polar side chain on the outside of molecule can interact with water and form hydrogen bonding. The non-polar side chains on the inside of the molecule forms a hydrophobic core. Interactions (can form when the folding begins) The interaction between the cysteine amino acids. Primary is identity of amino acids in a row. Interaction between the alpha helix and beta pleated sheets (secondary. Variety of functions that can be carried out. Multiple polypeptides join to form the quaternary structure. 1 chain of amino acid folding secondary structure (helix or sheets) The secondary structures can interact form a polypeptide multiple polypeptides interact quaternary structure (protein) Polypeptide can go as far as a tertiary structure. Quarterney is interaction of more than one polypeptide. If polypeptides interacted is more than one we use these names.
