NFS 033 Lecture Notes - Lecture 13: Maillard Reaction, Microscopic Reversibility, Glutamic Acid
28 Mar 2018
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Properly folded protein + denaturation (changes in ph or increased temp) -> denatured protein. Acidic = low ph // basic = high ph. Aspartic acid (asp) & glutamic acid (glu) = negatively charged, can gain proton. Histidine (his), lysine (lys) & arginine (arg) = positively charged, can lose proton. Acidic proteins are either not charged, or positively charged. Basic proteins are either not charged, or negatively charged. Coagulation meshwork of proteins held together by intermolecular noncovalent interactions (between different molecules) Folded proteins -> denatured proteins -> coagulated proteins. What thermal energy does to boil an egg, mechanical energy can undo. Adding heat disrupts the weak chemical bonds that hold together the protein in the egg, this process is denaturing. New bonds form, and lead to a boiled egg. The principle of microscopic reversibility, anything that happens can theoretically. By centrifuging the egg, the bonds return back to their native shapes.
