Structure for order of amino acids primary structure Structure for shape formed by hydrogen bonds between the carbonyl and the amino groups (e.g. beta sheets, alpha helix) secondary structure Structure for final shape of protein formed by variable R side chain tertiary structure Final structure of multiple proteins combine together quaternary structure Protein that contributes to structure like cytoskeleton, ECM, or spider silk structural protein Protein that performs a function functional protein Term usually used to refer to primary structure of protein peptide Bond between amino and carboxyl groups to create protein peptide bond Multiple amino acids bonded together to make polymers polypeptide Covalent bond that forms between two cysteine molecules disulfide bridge Number of amino acids 20 Location of protein synthesis ribosome Proteins that catalyze reactions enzymatic protein Proteins that help immune system detect and break apart pathogens by binding to antigen antibody Proteins used to store nutrients (e.g. egg white) storage protein Protein that signals to sell hormonal protein Protein that receives signals receptor protein Protein that moves contractile protein What is the entire set of proteins in a cell/tissue/organism called proteome Protein involved in absorbing carbon in photosynthesis rubisco Protein that regulates sugar intake insulin Glycoprotein that attaches to bacteria to identify pathogens by binding to antigens immunoglobin Protein that converts light into electrical signal for vision rhodopsin Structural protein found in skin, tendons, bones collagen What denatures proteins temperature ph Biological molecule that catalyzes one specific reaction without being used in the process enzyme The thing that binds with the enzyme substrate Part of the enzyme in which the substrate binds active site Result of chemical reaction with reactants in enzyme products Model in which shape of substrate matches shape of enzyme lock and key Model State in between products and reactants after Activation energy (E_a), unstable transition state Model in which enzyme clasps around the substrate when it binds due to changing bonds, stretching the molecule, bringing it into its transition state induced fit model Enzyme that breaks sucrose sucrase Enzyme that breaks proteins protease Enzyme that breaks lipids lipase Enzyme that builds DNA DNA polymerase Enzyme that can break down proteins in stomach pH pepsin Protein that breaks starch amylase Reactions that release energy are called exergonic Reactions that need energy are called endergonic Metals or other inorganic vitamins that facilitate movement of electrons not possible with side chains cofactors Thing that mimics substrate, slowing down Enzyme, but reversible by changing its concentration competitive inhibitor Thing that binds to the enzyme outside of active site to stabilize inactive shape, irreversibly making it slower or not work noncompetitive inhibitor Thing that can bind to enzyme to stabilize active shape activator molecule Thing where one activator can make all other subunits active, greatly increasing response cooperativity What factors create logarithmic graph where y axis is reaction rate substrate concentration enzyme concentration What factor creates normal distribution graph where y axis is reaction rate pH What factor creates left skew where y axis is reaction rate temperature Thing where enzymes are put into alginate beads or something else in high concentration (e.g. to make lactose free milk) immobilized enzymes What are organic cofactors called coenzymes Things that enzyme can change to catalyze orientation strain bonds environment What regulation is where noncompetitive inhibition is used allosteric regulation Regulation where result of a series of enzymes inhibits the first one, allowing a certain amount to be made feedback inhibition