BIOL 2020 Lecture Notes - Lecture 3: Tryptophan, Imidazole, Phenylalanine
14 Oct 2017
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Document Summary
More pure the acid base pair the better it is reactivity/stability is important. Ha+a = . 1mol/l x . 1 l = ,01 eq 2. Body/cellular buffers: phosphate, concentration of inorganic phosphate in blood is @1mm, proteins and peptides such as hemoglobin and albumin, carbonate buffer (most important) can alter and regulate ratios by breathing. Acidosis - ph decreases: drives reverse reaction. Alpha amino acids: building blocks of proteins, contains at least 1 carboxyl group and amino group, different side chains ( r ) or functional groups, 20 aa exist, alpha carbon (chiral) To have enantiomers must have chiral center: carbon with 4 different groups attached: polarize light. All amino acids in nature are in l form. Aliphatic - carbon linked together with open chain, not aromatic. Proline aliphatic but forms a ring not aromatic: side chain binds both alpha carbon and n of amine, bends in proteins. Phenylalanine - v hydrophobic bc just carbon and hydrogen.
