BIOM20001 Lecture Notes - Lecture 4: Christian B. Anfinsen, Globular Protein, Protein Folding
20 Jul 2018
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Where would you expect to find the various classes of amino acids in a folded globular protein? i. Nonpolar inside, polar outside (has to form h-bonds to reach lowest state of free energy- most stable) What forces drive protein folding and which amino acid type are involved in each type of interaction? i. ii. iii. iv. Electrostatic - ionised, polar (uncharged ones - dipoles) Vdw - between atoms to allow atoms to closely pack. Explain how did christian anfinsen"s experiments showed that under appropriate conditions protein folding/unfolding is reversible. How do protein folding chaperones help proteins fold in the cell? i. Help prevent misfolding - uses hsp70 machinery - chaperones attach to hydrophobic core. What is the thermodynamic basis of the hydrophobic interaction? i. Release of all the water surrounding it, increasing entropy. If you include all hydrogens, there are no empty spaces inside. Water is all around the protein, but not in the interior of the protein.
