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Biomolecules Ewald
| Term | Definition |
|---|---|
| lipid examples | fats, oils, waxes, steroids, pheromones |
| lipid characteristics | cushions organs, insulates the body, insoluble in water, long term energy storage |
| lipid monomer | glycerol and fatty acid |
| lipid polymer | triglyceride |
| saturated fat | solid, animal fat; ex-butter |
| unsaturated fat | liquid, plant oil; ex-olive oil |
| phospholipid characteristics | located in cell membrane (phospholipid bilayer); has a hydrophobic glycerol head and a hydrophobic fatty acid tail |
| monomer | one, simple building block |
| polymer | many, long chain, must be broken down into monomers to be absorbed by the body |
| carbohydrate functions | quick energy, cell membrane interactions, cell structure (cellulose) |
| carbohydrate monomer | monosaccharide; ex-glucose, fructose, deoxyribose |
| lipid shape | "E" |
| carbohydrate shape | chain of rings |
| disaccharide | 2 monosaccharides; ex-sucrose, lactose |
| carbohydrate polymer | polysaccharide; ex-plants use cellulose (long chain), animals use glycogen (branched structure) |
| nucleic acid shape | 3 parts:phosphate, nitrogen base, sugar |
| nucleic acid function | store and pass on genetic information, give the body instructions on how to make proteins |
| nucleic acid monomer | nucleotide (all 3 parts) |
| nucleic acid polymer | DNA-double stranded, has thymine (T), deoxyribose sugar; RNA-single strand, has uracil (U), ribose sugar |
| protein structure | chain of amino acids/ chain of circles |
| protein monomer | amino acid; there are 20 different amino acids |
| protein polymer | polypeptide |
| protein folding importance | must be folded correctly for the protein to work |
| protein folding order | 1-AA sequence; 2-alpha helix and beta pleat; 3-3D chain folding; 4-chains fold together |
| protein examples and functions | collagen-bone, cartilage; keratin-hair, skin, nails; antibodies-immune system; insulin-hormone to regulate blood sugar; hemoglobin-carries iron in the blood |
| enzyme function | speed up chemical reactions by lowering the activation energy |
| catalyst | enzyme used in the body |
| enzyme/catalyst examples | lipase, sucrase, lactase, amylase (always end in -ase) |
| lock and key model | enzyme and substrate are specific to each other; one enzyme for one substrate |
| active site | where substrate binds to an enzyme |
| substrate | reactant that binds to the active site of an enzyme |
| enzyme-substrate complex | when enzyme and substrate are bound together |
| product | after enzyme has done it's job, a new product is created in the reaction |
| denature | when an enzyme changes shape by breaking the 3' bonds; caused by temp or pH changes; irreversible |
| competitive inhibitor | another chemical blocks the active site; substrate can't bind; may make the enzyme unusable |
| coenzyme | make the enzyme go even faster; ex-vitamins |