Proteins carbonshydrogensoxygensnitrogensmonomers ofproteins functionalgroupsaminoacids20possibleamino acidtypes 20different Rgroups11 nonessential madebycellsbaseaminoacidsare bondedbypeptidebondsacid formpolypeptidechainsformfromdehydrationsynthesisaminoacidsdifferdue tovariable R group remove H2Ofromcarboxygroup t amino groupazoIfÉEntÉ Epeptidebondaaminoacidsdipeptidesoaminoacidsoligopeptide20 aminoacids polypeptidespecialcasesexplainedcysteine Han i coo prolineIg as groupwinform own pigbondwothercysteineside The C aminogroupmissingan itallowsaminoacidtofitchain disulfidebridge in jiff easily causingcovalentbondtoformprotein functionsfunctionalenzymes acceleratebiochemicalruns salivaryamylase keratin fingernails hairfeathershormones regulatoryinsulingrowthhormone collagen connectivetissuesligamentsbonesskintransportother substanceshemoglobin carrieson elastin skinelasticitypmyosin structuralandfunctionalmusclemovementProtein structures1 primarystructure polypeptideEgg peptide ten hydrogenbondingbeginsresultinginalphahelixorbetapleatedsheetbond betweenn it co of backbonew nonotaproteinyet proteinhasfunction examplemyoglobin alwaysonly2structureamino acidsequence a helixpyftwistedbackbone psheetwilldeterminehowprotein foldsmanIitbondstoholdshape 3tertiarystructure3Dgobularshape madeof 2 polypeptidechainstertiarybondingfromsidechain interactions nolonger 1 aminoacidsequenceioniccovalenthydrogendisulfidebridges examplesmostcomplexstructureforsinglepolypeptide hemoglobin bloodproteinmadeof 4polypeptidechainsused to carryor in redbloodcellscollagen fibrousproteinTertiary Quaternarymade of 3 polypeptidechainsDenaturationstrongaciddenaturingcanonlyfullyresolve if primarystructureis not disruptedwhenproteins losetheirstructuralshaperesultsin lossexamplesofirreverserabledenaturing offunctionalpropertiescookingcrab milkcurdlinganditturning duetoexternalexcessiveacidpink stresscompound LargedenatureHt presencesmalldenaturesmalllossofexcessiveheat largeloss of functioncausingdenotruationcausingdenaturation examplephorbase