Human Biochemistry BMOLCHEM 503
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This 2 page Class Notes was uploaded by Mabelle Gaylord on Thursday September 17, 2015. The Class Notes belongs to BMOLCHEM 503 at University of Wisconsin - Madison taught by John Denu in Fall. Since its upload, it has received 27 views. For similar materials see /class/205238/bmolchem-503-university-of-wisconsin-madison in Biology Molecular Cell & Dev at University of Wisconsin - Madison.
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Date Created: 09/17/15
Review of topics for Biochemistry Fundamental concepts in biochemistry throughout science and medical career Lec 1 Macromolecules that control cellular function polysaccharides DNA RNA lipids proteins Functional groups refresher o chem Concepts cysteins serine histidiene in acid base catalysis Weak interactions between molecules and with a particular molecue as in a protein Hydrogen bonds ionic interaction hydrophobic interaction van der waals interaction Lec2 Chemistry of qater and behavior of polar in water Weak acids and weak bases Henderson hasselbachs equation Ph pk plus log A HA Pka values of R and Amino Acids Electrostatic rxn wanna a carboxylate negative and lysine positive charge a stable ionic bond charge Aprox Pka values should know Study aids are important at the end Should answer very quickly and list of 12 AA know the structures listed in study aid 3 Recognize arg and tryptophan Know the 3 letters or whole name Lec 3 Protein structure Beta strands and alpha helices are secondary structure Homo dimmer and heterodimer are representative of quat Protein folding kinetic and thermodynamic perspective K how quickly T whether it will happen in the direction shown Folded structure more stable than unfolded Protein can spont fold Inherent in the primary sequence Scientist make a good prediction in the region where there will be alpha helices or beta sheeths from the primary structure by computer algorythems Harder to predict tertiary structure Here would you find proline good at making turn folding back on itself good AA as well as Glycine bc a lot of conformation entropy and oppier regions of the secondary struct Lec 4 Protein function assist as structural bricks and mortar in offering an organims overall structure Collagen Immunoglobins not an enzyme but involved in host defense recognized foreign invaders Proteins involved in transporting across a membrane How to discuss what a membrane is and lipid membranes Difficulty in transporting a membrane that is highly charged and evolutionary uses a specific transport Down conc gradient passive transport Pump across membrane up conc gradient active transport ATP hydrolysis to drive a molecule against the conc gradient Cost energy Phospholipid is ampiphatic greasy chain tail and a polar head group 2 sides with different functional group Lec 5 Hemoglobin and myoglobin Continuation of transport proteins and oxygen binding proteins Know the similarites differeces Behavior in respect to binding oxygen Hemo is an allosteric complex protein Hemo existing in R and T state one binds oxygen readily R and one does not T Contributing factors BPG pH C02 Lec 6 Proteins as catalysts and enzymes Enzyme cascades Zymogen inactive precursor of a protein or enzyme Cleave protelytically to make enzyme Think digestive enzymes in the gut Protease cascade that initiates blood clotting Amplification required at each step of the enzyme cascade as one enzyme activate another exponential increase critical when stop losing blood Vit K dependent processes Gamma carboxylation of gultamanate Blood clotting modifications are irreversible modification in terms of controlling enzyme functions Which contrast with reversible modification of hydroxyl groups ofprotein acetylation lysine Lec 7 Basic properties of enzymes Catalytic strategies 5 Used One of the 5 is always true proximity and orientation Active site is set up to bind on the substrate exserine protease his is posed to activate ser residue Huge entropy cost Know the other 4 Chymotrypsin cool mechanism know 1 of the genome serine protease and catalytic triad Cysteine protease don t have asparytl acid Aspartly protease metallo protease Activate a water molecule to directly attack a peptide bond Enzyme nucleophile to attack the carbonyl than water attacks for ser cys protease Lec 8 Steady state function substrate is present in excess over the enzyme the later rxn wshould be linear with time Derivation of the michaelis menten saturation V Vmax S Km S the Km is half ofvmax Y int v X is substrate concentration Slope is km vmax Lec 10 compettive inhibitorand unompetitive inhibitornon mixed Think physically Ezyme drug interactions Mechanism based inhibitor is taking advantage of catalytic mechanism or compliment to active site HIV protease aspirin acetylcholine esterase inhibition penicillin Lec 11 Enzyme regulation effector molecues small allosteric molecules Post translational modification irreversible and reversible modification phosphorylation and acetylation Lec 12need to couple unfavorable rxn with favorable rxn to create a lot of energy in the process Oxidation and reduction reaction NAD and FAD TCA cycle soaking up electrons Structure of glucose and rxns of glycolysis know Study aids for lec 11