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University of Toronto St. George
Dave Tulumello

LECTURE 02Peptide rotational angles 3 typesphiangle around the Nalpha C bondpsiangle around the alpha CCO bondomegaangle around the CN bondchi angles reserved for side chain rotationalpha helix phi psi 60 degrees 50 degreesbeta sheet phi psi140 degrees 135 degreespolyproline helix phi psi60 degrees 135 degreesLresidues in proteins has 25 phi psi space normally populated oEX Glycine75Fibrous proteinsEX SilkoRepeats of glyserglyalaglyalaBetasheetsInterchain hydrogen bonds formed while side chains are above and below the plane of the hydrogenbond network Easy for packing Strong fibres that resist tension via covalent bonds Fibrous proteins include keratinsoThey form hair wool etc oHave fewer glycines than silk oEven distribution of helixforming residues also collagenopolyproline helix fundamental unittriple helix oa third glycine glycine in every third position ouniversalorigid inert stretchresistantofound in connective tissue skin tendons wool opossible to stretch to twice its length when stretched intrahelix hydrogen bonds can be broken and interstrand hydrogen bonds formvia alphahelix to betasheet transition sulfur presentdisulfide crosslinks help restore to original shape Resonance structures give CN bond partial doublebond characterPeptide bondresonance hybrid of two extremes thus bond is planaroPartial doublebond character oDihedral angle omega fixedoPlanar AND trans
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