Proteins

• Proteins are made up of an Amino Group, a Carboxyl Group and a R group
• Proteins are joined with Peptide bonds
• Primary structures are the order of amino acids in a polypeptide chain
• Secondary structures are bent/folded into Alpha Helixs or Beta Pleated Sheets with hydrogen bonds
• Tertiary structure is the 3D structure of a protein formed with Ionic, Hydrogen and Disulphide bonds
• Quaternary structures are formed by the interaction of multiple polypeptide chains
• Enzymes are tertiary structures, they are biological catalysts that speed up chemical reactions by lowering activation energy
• Active Sites are unique due to the tertiary structure determined by the primary structure, complementary to the shape of the substrate
• The Induced Fit Model is when the active site is induced, slightly changing shape, to mould around the substrate, forming an E-S complex that puts strain on bonds and lowers Activation Energy
• Temperature is a factor affecting enzymes, low temp doesn't provide enough kinetic energy for successful collisions, high temp denatures enzymes breaking bonds and changing active site
• pH is a factor affecting enzymes, interferes with the charges of the amino acids in the active site, denaturing it by breaking bonds and changing shape
• Substrate-Enzyme concentrations are factors affecting enzymes as there are fewer collisions, a saturation of one factor will decrease the rate of the reaction
• Competitive inhibitors are similar shapes to substrates, binding to the active site preventing E-S complexes
• Non-Competitive inhibitors bind to the allosteric site, changing the shape of the active site preventing E-S complexes