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Where are amino acids linked? In living cell Ribosomes! These reactions that occur on the ribosomes are controlled by ENZYMES (more on this later) How are polypeptides broken? Hydrolysis Reactions Naturally occurs in stomach and small intestine Protein in food is hydrolyzed into amino acids prior to being absorbed by the blood Once in the blood, these AA can be restructured into polypeptides and then twisted and folded into functioning PROTEINS the cells in you body needs Protein Structure Primary structure 1’ Order of amino acids in a polypeptide chain Secondary structure 2’ Polypeptide chain folds because of interactions between amino acids HYDROGEN BONDING Tertiary Structure 3’ Gives proteins 3-D shape VERY IMPORTANT to function of protein Beta pleated sheets and alpha helices fold based on interactions between R-groups of a.a. Hydrogen bonds, polar/non-polar interactions, acid/base interactions, disulfide bonds, van derWaals forces Quaternary Structure 4’ the association of the polypeptide chains some proteins contain more than one polypeptide chain Each polypeptide chain in the protein is called a subunit Two or more subunits come together for a specific function HEMOGLOBIN On Red blood cells Its shape allows RBCs to carry oxygen all around your body! Practice Set 6 Primary Structure Sequence of AA in a long polypeptide chain AA= letters of alphabet Sequence of AA= arrangement of letters to make words HUGE amount of different primary structures Changing ONE AA is polypeptide chain GREATLY changes the properties of the polypeptide chain and PROTEIN Secondary Structure The order of AA in polypeptide chain determine interactions between functional groups of AA Functional groups interact via HYDROGEN BONDS Attraction between oxygen in the –CO end of one AA and the hydrogen in the – NH end of another AA H-bond easily broken Change pH and change Temperature Three possible 2o structures Determined by order R-groups No particular arrangement Alpha helix Polypeptide chains that coil tightly Beta pleated sheet Looser, straighter shape created by hydrogen bonds Tertiary Structure Secondary structure gets coiled and folded Precise 3D shape Folding is determined by interactions between R-groups Hydrogen bonds Tryptophan Arginine Asparigine Disulphide bonds Between 2 cystine molecules Ionic bonds b/t R groups containing amine and carboxyl groups Hydrophobic interactions b/t R groups that are non-polar (hydrophobic) 2 main types of tertiary structures Globular form ball-like structures where hydrophobic parts are towards the centre and hydrophilic are towards the edges Structure=water soluble Found in watery environments o cells, tissue fluid, or in fluids being transported (blood or phloem) metabolic roles Ex: enzymes in all organisms, plasma proteins and antibodies in mammals Fibrous form long fibres mostly consist of repeated sequences of amino acids which are insoluble in water usually have structural roles Ex. Collagen in bone and cartilage Keratin in fingernails and hair Quaternary Structure Proteins are made up of multiple polypeptide chains, sometimes with an inorganic component (for example, a haem group in haemoglogin) Prosthetic Group (inorganic component of protein) These proteins will only be able to function if all subunits are present Made by same bonds found in tertiary structure Interactions between R-groups Hydrogen bonds Tryptophan Arginine Asparigine Disulphide bonds Between 2 cystine molecules Ionic bonds b/t R groups containing amine and carboxyl groups Hydrophobic interactions b/t R groups that are non-polar (hydrophobic)