BCHM-3050 Lecture Notes - Lecture 19: Globular Protein, Alpha Helix, Beta Sheet
9 Jul 2018
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Document Summary
Tertiary structure and folding diversity: most of the chemical work of the cell (transporting/metabolizing) is done by globular proteins, their polypeptide chains are folded into compact structures, which can either be alpha helix or beta pleated sheet. Tertiary structure: globular 3d structure of a polypeptide that results from folding and interactions with the other secondary structures, myoglobin is an example. It binds to heme and is made up of 8 different alpha helices: structure defines function, tertiary structure of a globular protein is the major determinant of its functional properties. Chemical interactions that stabilize tertiary structure: hydrophobic interactions. ** proteins bury non-polar side chains on side and polar side chains on the outside: electrostatic interactions, hydrogen bonds, covalent bonds. Tertiary models: cartoon model: show the backbone structure, and see if it"s a helix, loop, or beta, stick model: all atoms are shown. Cannot tell side chain atoms from main chain atoms.
