BIOC 3560 Lecture Notes - Lecture 1: Protein Structure, Porphyrin, Flavin Mononucleotide
13 May 2016
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Protein structure properties: size, shape, charge, hydrophibicity / hydrophilicity. Protein structure vital to understanding it"s function and biochemistry. Protein function dep. on it"s interactions (stable or transient and short-lived) w/other molecules. Stable interactions incl. prosthetic groups: a cofactor permanently associated w/a protein, req"d for it"s fxn. Protein structures represented in multiple ways to show different things (same protein, different views): Understand how a protein works by looking at it at the atomic level. If the structure were changed by 0. 5 , could lose all enzyme activity. Instantly explains a lot of biochemical effects i. e. how life processes work (health) and why they sometime"s don"t (disease) Function influenced by interactions with other molecules. Prosthetic group: a compound/cofactor that is permanently associated with a protein and required for its function e. g. fad, fmn, iron porphyrin groups of hemoglobin. Ligand: a molecule bound reversibly by a protein. Binding site: position on protein that interacts with a ligand.
