BCHM 3050 1st Edition Lecture 9 Outline of Last Lecture I Tertiary Protein Structures II Quaternary Protein Structures III Unstructured Proteins IV Protein folding V Anfinsen Experiments VI Denaturation VII Molecular Chaperones VIII Protein Degradation IX Diseases Associated with Misfolded Proteins Outline of Current Lecture I Mad Cow Prions II Fibrous Proteins III Collagen IV Globular Proteins Myoglobin vs Hemoglobin V Oxygen Binding Equilibrium Curves VI Effects of pH on Oxygen Binding Current Lecture I Mad Cow Prions These notes represent a detailed interpretation of the professor s lecture GradeBuddy is best used as a supplement to your own notes not as a substitute a When consume undercooked meat can consume these misfolded proteins and cause more misfolding b Pre prions covert to prions which can fold abnormally c A lot of unnecessary beta sheets in misfolded prions II Fibrous Proteins a Fibrous protiens main function is structural support b Enzymes are generally not fibrous c Keratin is rich is alpha helices KNOW THIS d Silk fibroin forms spider webs is a fibrous protein rich in beta sheets e Simple do not usually form a tertiary quaternary structure III Collagen a Collagen has left handed alpha helices that twist in a way that they assume an overall right handed conformation b Glyines and prolines are usually not found in alpha helices only in turns but they are found in these left handed alpha helices abnormal case c Early on in the collagen life lysine basic amino acid and lueine nonpolar are able to create crosslinks support flexible d With age the connections are lost and before softer wrinkles e Skin age products try to work on how to prevent the loss of these crosslinks IV Globular Proteins Myoglobin vs Hemoglobin a Same prosthetic group i Prosthetic group like a co factor help protein to do its job ii Iron is the core of the prosthetic group and the amino acid next to iron is histidine b Very similar function c Myoglobin is a monomer hemoglobin is a tetramer d Blue blood hemoglobin devoid of oxygen e Red blood hemoglobin with oxygen RBCs are rich in oxygen f Hemophilia anemia and hemoglobin is not able to retain oxygen instead it is saturated in CO2 g Blood unloads oxygen in tissue need myoglobin in tissues to accept oxygen and slowly release it over time h Hemoglobin more active in the lungs i Myoglobin more active in the tissues j Both can accept oxygen k hemoglobin s lower affinity to oxygen enables it to release the oxygen to myoglobin in the tissues l Myoglobin only has one binding site for oxygen m Hemoglobin has multiple oxygen binding sites n More binding sites less affinity o Less binding sites more affinity V Oxygen Binding Equilibrium Curves a Myoglobin hyperbolic curve stronger affinity for oxygen b Hemoglobin sigmoid curve lower affinity for oxygen VI Effects of pH on Oxygen Binding a Ex workout a lot pain in muscles lactic acid accumulation due to depletion of oxygen lowers pH hemoglobin cannot get to oxygen b Lower pH dissociates hemoglobin from oxygen
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