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Dave Tulumello

LectureSeptember 23 2011 Protein folding Unique biological structurehow formedDipeptide can be four hundred possibilitieso Amino acidshuge number o As protein chain gets longer Just been synthesizedo Protein begins to fold into functional sturcutre taking into account info in sequence and interactionso Paradoxhow come it takes so short amout of time to fold when theorized to be so longDirected folding Directioning caused by sequence Early steps in protein folding Statistical polymerunfolded chain Transient alpha helices form theno Made up of amino acids that have side chains that are conducive to formation of alpha helix or relatively hydrophobic amino acids that will end up in the middle of the final globular protein Two distinct regions of protein form secondary structure Then statistically speaking these helices will come into contact with each othero Van der waals packing can guide this processo Two helices stabilized by interactions btw them Short beta sheet structureboth will come together and form stabilized structure Nucleation of structurethen rest of structure begins to fill in Yellowhalf way through folding processo Some loops appearingo Some interactions between side chainso At this step what happens next How proceedProtein is sampling all the possible non covalent directions ranging from hydrogen bonds to van der waals packing until reaching final structure that is sum of all interactions that when added up bring the protein to lowest energy or most stable Folding of ribonuclease A Anfinsen tried to prove this idea since folding is directed what else but amino acids doing the directingUsed enzyme ribonuclease Consider all protein interactions including directing disulfide bonds ribonuclease has fourRibonuclease Hisitidine 12 lys 41 his 119o Lys 41 his 119 o Four disulfide bonds scattered throughout proteinReduction of the disulfide bonds in a protein byBeta mercaptoethanol has SH group
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