← chapter 3 vocab BIO Export Options Alphabetize Word-Def Delimiter Tab Comma Custom Def-Word Delimiter New Line Semicolon Custom Data Copy and paste the text below. It is read-only. Select All lipid consist of mainly carbon and hydrogen atoms, linked by non polar covalent bonds, hydrophobic hydrophobic water fearing triglyceride linking 3 fatty acids to a glucose, fat glycerol an alcohol with 3 carbons, each with a hydroxyl group fatty acid consists of a carboxyl group and hyrdrocarbon chain, 16,18 unsaturated fat fatty acids and fats with double bonds in the carbon chain saturated fats with max # hydrogens cis N trans W hydrogenated un saturated fat gets converted into saturated by adding hydrogen phospholipid major component of cell membranes, contain 2 fatty acids attached to glycerol. instead of third carbon, it is replaced by negatively charged phosphate group bilayer what allows phospholipids to form membranes. hydrophyllic and phobic ends of lipids whose carbon skeleton contains four fused rings steroid lipids whose carbon skeleton contains four fused rings cholesterol common component in animal cell membranes, and animal cells use it to make steroids like sex hormones protein polymer from amino acid monomer enzyme chemical catalysts that speed and regulate all chemical reactions in cells amino acid amino group and carboxyl group. covalently bonded to central (alpha) carbon alpha carbon central carbon in amino acid peptide bond covalent linkage when amino acids bond. cells join amino acids together in a dehydration reaction that links the carboxyl group of one amino acid to another one as a water molecule is removed dipeptide product of two peptides bonding polypeptide a chain of amino acids denaturation a process where polypeptide chains unravel, losing specific shape and function. occurs because of excessive heat, changes in salt, or pH denature to unravel polypeptide chains primary structure unique sequence of amino acids in a protein secondary structure parts of polypeptide coil or fold into local patterns tertiary structure 3 dimensional shape of polypeptide quaternary structure proteins with two or more polypeptide chains have quaternary structures based on the association of subunits alpha helix coiling of a polypeptide chain beta pleated sheet One form of the secondary structure of proteins in which the polypepetide chain folds back and forth. two regions of the chain lie parallel to each other and are held together by hydrogen bonds.