BioChem Week 6
BioChem Week 6 CHEM 3653 - 001
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This 4 page Class Notes was uploaded by Lauran Notetaker on Tuesday March 29, 2016. The Class Notes belongs to CHEM 3653 - 001 at University of Oklahoma taught by Dr. Paul A. Sims in Winter 2016. Since its upload, it has received 9 views. For similar materials see Biochemistry in Chemistry at University of Oklahoma.
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Date Created: 03/29/16
February 23, 2016 Chapter 6: The Three-Dimensional Structure of Proteins Levels of Protein Structure Primary (sequence of amino acid residues) Secondary Tertiary Quaternary - Protein with one or more structural units 1.45A 1.33 1.25A -1.25 0.08 = 40% 0.2 0.08 0.2 Ramachandran Plot Phi and Psi bond angles be concerned with Alpha helices and Beta strands Discoverers of the Alpha Helix Linus Pauling Robert Corey C-terminal g- N-terminal g+ The Alpha Helix right handed 3.6 residues 5.4A pitch intramolecular C=O and N-H 4 residues ahead in helix side chains splayed out Beta strands and sheets sheets are more than one strand Antiparallel C N C N C N C N 2 residues span 7.0A polyproline II helix is left-handed Fibrous Protein Structure silk keratin - hair, ﬁngernails The intermediate ﬁlament protein Alpha keratin Two right handed alpha helices intertwine to form a left-handed super coil Collagen abundant in connective tissue if you don't hydroxylize proline coil it wont be as tight NMR - Nuclear Magnetic Resonance Globular Proteins, typically fold into deﬁned structures Triphosphate Isomerase (TIM) February 25, 2016 Homework 7 moved to Next Thursday Hydrophobic side chains inside of protein are non polar Polar (charged) face toward surface of protein “zinc ﬁngers” cysteines and histidines Christian Anﬁnsen and Bovine Ribonuclease A - RNase can still act as an enzyme unfolded? No need to keep shape (folded) found that most of the info specifying the tertiary structure is carried in the amino acid sequence Protein Folding Thermodynamics Proteins vary in the extent to which the folded state is favored by enthalpic or entropic factors Disulﬁde bonds greatly increase stability Levinthal’s Paradox and Dawkins Typing Monkey once you type a key, you keep it Chaperones promote proper folding of proteins and thereby prevent the formation of aggregated states associated with disease -Ex. Alzheimers Dangers of misfolding Alzheimers disease Parkinson’s disease Type II Diabetes Cataracts Can we predict secondary structure from amino acid sequence? Empirical methods are ~ 80% accurate Chapter 7: Protein Function and Evolution “Derivation of Protein-Ligand Binding Equations” Keq = [PL] = k2 [P][L] k1 (Where the k1,k2, and k3 come from are on the handout mentioned above) He is not going to ask detailed questions about the biology of antibodies antigen binding sites antigen bonds to antibody and interactions are mediated by shape and charge Gobins (Mb) myoglobin is monomeric, releases O2 in tissues (Hb) Hemoglobin is tetrameric, transports O2 from lungs to peripheral tissues Heme is an Irom Porphyrin Mb or Hb without heme is called apoprotein with heme is holoprotein O2 binds at the heme Fe2+ oxygen binding curve for myoglobin Y= [L] Kd+[L]
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