mastering biology chapter 3

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differs in covalent bonds between atoms
differs in the arrangement of atoms around a double bond
molecules that are mirror images of each other
-varies in length
-varies in number & location of double bonds
-can be branched/unbranched
-can be arranged in rings
-O bonded to H
-needs to be bonded w/ a carbon skeleton
organic compound that contains a hydroxyl group (i.e. ethanol)
-C double bonded to O
-can be located within or at the end of a carbon skeleton
-works w/ carboxyl groups to make sugars
organic compound in which the carbonyl group is attached at the end of a carbon chain
organic compound in which the carbonyl group is attached to a carbon atom within the carbon chain
-C double bonded to O and single bonded to a hydroxyl
-acts as an acid by donating H+
-found in all proteins
organic compound that contains a carboxyl group
-N bonded to two H atoms
-acts as a base by picking up H+ from a solution to become ionized (NH3+)
-found in all proteins
compound containing an amino group
-Organic compounds containing a central C bonded to an H atom, amino group, carboxyl group, and R group
-R-group that projects from the backbone makes each amino acid unique
-Building blocks of proteins
-P doubled bonded to O single bonded to 3 O atoms
-acts as an acid, losing H+
-organic compound containing phosphate groups
-involved in energy transfers (ATP)
-S bonded to H
-groups can react & form a crosslink that stabilizes the structure of many proteins
organic compound that contains a sulfhydryl group
-C bonded to 3 H atoms
-organic compound that contains a methyl group
-component of DNA that affects gene expression
-covalently bonding monomers to form a polymer through the removal of H2O (H and OH)
-energy can be stored when the bonds are formed
-chemical reaction in which bonds between molecules in a polymer are broken down by the addition of H2O to form monomers (H and OH)
-energy is released when the bonds are broken
-contains C, H, O, N, P
-polymer made of nucleotide monomers
-sequence of nucleotides carries information
-Polymer that stores hereditary information
-Single molecule contains 2 polynucleotides
-Double helix formed by the twisting of 2 complimentary strands of nucleotides
-Backbone consists of alternating sugars and phosphates
-Strands are held together by hydrogen bonds between pairs of nitrogenous bases
-Polymer that synthesizes proteins
-Consists of a single-stranded polypeptide
-Contains ribose
-Uracil instead of thymine
-Copied from a DNA molecule
-Shorter than DNA
-building block of DNA/RNA
-consists of a five-carbon sugar (deoxyribose/ribose), nitrogenous base, and a phosphate group
-polymer of nucleotide monomers
-backbone consists of alternating sugars and phosphates
-bases are attached to the sugars
-contains C, H, and O in a 1:2:1 ratio
-used as fuel for cellular work (form of immediate energy)
-form of glucose
glycosidic bond
cellulose (fiber)
triglyceride (fat molecule)
ester bond (ester linkage)
-glycerol bound to 2 fatty acid tails and phosphate group
-forms cell membrane
-hydrophobic fatty acid tails face inward, mingling together
-hydrophilic heads face outward, exposed to aqueous solutions on both sides of the membrane
vitamin D
fatty acid
-Contains at least one double bond (kink) in their hydrocarbon chain 
-Reduced number of H's
-Usually found in vegetable oils
-Liquid at room temperature
-Stimulates the breakdown and secretion of cholesterol.
-Contain only single bonds in their hydrocarbon chains
-2 to 3 H's on each C
-Found in animal fats
-Solid at room temperature 
-Impede the excretion of cholesterol
-Stimulate cholesterol synthesis in the liver
-Formed by double bonds
-Prevents fatty acids from packing tightly
-Keeps them liquid at room temperature
-unsaturated fat formed during hydrogenation of saturated fat
-contain fewer double bonds
-linked to health risks (i.e. heart attacks)
process of adding hydrogen to double bonds
-Linear string of amino acids that forms the backbone of the polypeptide chain
-Determined by genetic info
-Local patterns or folds of a polypeptide chain between amino & carboxyl groups
-Caused by interactions between R-groups
-Overall globular (3D) shape of a polypeptide due to interactions of the R groups of the amino acids making up the chain
-Hydrophobic R-groups cluster in the center
-Positively/negatively charged R-groups can form ionic bonds
-Polar R-groups can form hydrogen bonds
-Sulfur-containing R-groups can form covalent bonds
-2 or more individual polypeptide subunits
-not present in all proteins
-the unraveling of a protein, losing its structure and function
-the separation of 2 strands of DNA
-caused by changes in pH, salt concentration, or temperature
transport proteins
structural proteins
signal proteins
sensory proteins
storage protein
contractile protein (motor proteins)
gene regulatory protein
-covalent bond between an amino group of one subunit w/ a carboxyl group of another subunit
-formed by dehydration