BIOL 2050 Chapter Notes - Chapter 4: Protein Folding, Amine, Peptide
Document Summary
~proteins are linear polymers of any combination of 20 amino acids. ~amino acid- central carbon atom connected by covalent bonds to four. 4. 1 molecular structure of proteins chemical groups (amino, carboxyl, hydrogen, r) ~proline-r group is linked back to the amino group, kink restricts rotation. ~cysteine- makes contribution to protein folding through its sh group. ~secondary structure- interactions between stretches of amino acids in a protein. ~tertiary structure-longer-range interactions between these that create a. ~quaternary structure- proteins made of several individual polypeptides. ~a helix- polypeptide backbone is twisted tightly with amino acids, r groups project outward from the a helix. ~b helix-r groups project above and below the plane of the b sheet, ~tertiary structures result from interactions between amino acid side chains- spatial distribution of hydrophilic and hydrophobic r groups, determines structure. ~polypeptide subunits can come together to form quaternary structures- the influence of different subunits together.
