Proteins GapFill

Amino acids are the monomers which form  nucleic acidstriglyceridesphospholipidsproteins. There are  thirty twosixteenfourtwenty common amino acids found in organisms, all with the same basic structure of an amine group and  a phosphatean alkenea carboxylan alcohol group, but they differ in their R groups, or side chains.

Polypeptides are formed by  condensationmultiplicationhydrolysisreduction reactions, where many amino acids form a chain linked by  peptidedoublehydrogenglycosidic bonds. This sequence of amino acids is known as the primary structure. Interactions between slightly positive hydrogens and slightly negative oxygens are called  hydrogen bondswater bondsionic bondsoxygen bonds, and these result in a chain twisting into  an alpha helixa double helixan omega springa peptide plait, which is the secondary structure. Further twisting and folding into the tertiary structure can occur as a result of ionic bonds and  disulfide bridgesamino bondscarbon pathscovalent tunnels, and sometimes more than one polypeptide chain may come together as the  fourth sequencequaternary structurecombinatory peptide formfinal form of the molecule.

Enzymes have specific 3D structures that result in the formation of an active site, a region where  an activatora basea substratea product can bind in  permanencea hydrophilic channelan induced fita lock and key fit. Enzymes lower the  pressurewater potentialtemperatureactivation energy of reactions, which speeds up the rate when they are present. However, their effectiveness can be compromised; for example, if a  lownon-optimaldecreasingincreasing pH or temperature is used, enzymes become  brittlegelatinousdenaturedexhausted. They are also susceptible to competitive inhibitors, which block their  poressecondary structuresactive sitessequence ends, and non-competitive inhibitors, which change their overall shape.