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BCH210H1 (352)
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Department
Biochemistry
Course
BCH210H1
Professor
Dave Tulumello
Semester
Fall

Description
WEEK 3 BCH210 Protein folding Linear chain of amino acids to final structure of proteincalled protein folding the processLevinthals paradoxbasically proof that folding must be directed in some methodIf fold randomly on their own proteins probably wouldnt actually fold take too long Anfinsens postulateIdea that primary sequence enough to determine overall structure Nucleation secondary structureSome part of primary structure forms a secondary structurequickly done Backbone can only take one of few conformationsHydrophoic effect dominant in foldingo Help form structure o Collapse of small units small secondary units driven by hydrophobic effect beginning nnucleation of tertiary structureo Helices stable stabilized by hydrophobic effecto Final folding of other residues Certain regions are formed first because more stable rest are formed upon thatHappen with alpha helices beta strandseven combination of bothcan be first things formedRibonuclease AAnfinsen Proteins activitycan look at activity when active must be folded properly o Not folded properly wont function Also have disulfide bondsthought to stabilize structure what role such bonds playUnfolding a protein Denature the proteino Heatlow energy makes structure protein stable los of energy around unstable o Use chenicals that compete for native interactions Urea looks like peptide bondHave lots of hydrogen bonding potential Lot of urea more than protein protein cant form well instead of forming hydrogen bonds iwth amino acids to form secondary strcture will bond with ureaSo disrupt secondary structure y Proteins need secondary structure to form before tertiary so if disrupt secondary structures unfold protein BetaM y Sulfur attach dot hydrogenlike in cysteine y Form disulfide bonds with bmerca instead of other cystines in proteino Scramble disulfidesForm with different partnerFolding a protein vi
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