Proteins BCH-1.05 PDF
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CCNM | Canadian College of Naturopathic Medicine
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Summary
This document presents lecture notes on protein structure and function. It covers topics such as protein classifications, shapes, structures, and the ubiquitin pathway. The document also details protein denaturation methods and the processes of protein degradation emphasizing methods of enzyme regulation.
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Proteins Structures Shape is everything which is dictated by a a sequence a As thissame as he deprotonated molecules studied Aff earlice Listen Eg of Hemoglobin Myoglobin ...
Proteins Structures Shape is everything which is dictated by a a sequence a As thissame as he deprotonated molecules studied Aff earlice Listen Eg of Hemoglobin Myoglobin end aminoTerminalendtoc.la depends on how backboneis Inβsheet oversensitive of varione protein Subunits interact howvarious interact 2 α and 2 β howthey eg Check text book RBC _When a cell dies hemoglobin is free in plasma Itthendissociates into 2 subunits α β units It then be leptogo β a picked up listen oomimbook verystrongbond ooo ama R's stink all R groups outside Prolene is an x helix breaker Party't butcan be fn interption no coil A schematically c a 0 I Beta Totene has to be beta alpha stretched polypeptid hereas it's a helix interacting with for breaker away segments of eachother confirm Mm SH groups are oxidised stabilize structure chains in Aand B eg Insulin Valene Aminotaminal Nitz cootte C terminal Aterminal acid salt group cterminal ionicbond apart cytine POLYPEPTIDE CHAIN filfide group try to bond with other sulfides stabilizes In Insulinmade in β all of liver btwchain intermolecular imp part state fed Listen Receptor Noreceptor noresponse There are insulin receptors initiate Intotal 4subunits 40xygonbinding Oxygenbindingchangesshape a subunitsthat subsequently of subunits changes structure oftherest of Binding of 0 change of shape of hemoglobin One Subunit Monomer Probably 3 10 Kane is a multimer py Erething µ 2 α subunits subunits 2 β Myoglobinstores 02 in muliertissue Hemoglobin transports 02 Bothcan worktogether in appropriate situation 2 types 1 A µ eg Insulin methyanine example addition of Carbohydrateto proteinaffecting protein happening all thetime properties of areentymatic I activityspedupor sloweddown Adding or removing Oligomore or Phosphorus Binding ATP Changer slate allosteric state of enzyme PFK once broken peptide bond won'tjoin again connectedpeptide is removed the Ipart arehittin zymogen In dig cys profiti enzymes in did so a a Efim i5 meat artist Pepsin alsozymogen addition Carbohydrate A Carbohydrate A Carbohydrate W Glycotsylation All cytosol outsidecell in µ negatively charged ion Adrenaline orprevent removed once they have helped theprotein Glucokinase remain in cytosol Hexokinase Membrane bound protein has hydrophobic nature and it will were to incorporate in acid fatty ᵈ o ffa example ofsystem Digestive N o amount is crucial µ w metal ionic bonds broken in presence of heavy disrupts RBC and formation of Lead binds to sulfide group hemoglobin we end up with anemia Leadfrompipes still teacher over time Heavymetals don't affed immediately They work IT mapuaa afeiagntttaig.it afesetting membrane This has to be very controlled no cars system as removed protein has to be replaced Howdoes it diagnose or recognised bondprotein mechanismmon µ P ketone body oxidized need milo matrix to A transferace Takes CoAtransferase is low The level of A transferase in cells several days If fasting starts to be induced outside liver m RNA will be made it will be synthesised Liver can Liver no CoAtransferase induce make but not break ketone bodies Control liner need to make glucose fasting need to be induced enzyme for glucogenesis then
