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CP BIOLOGY Chapter 2 Review BIOMOLECULES Name __________________ These are topics and vocabulary terms covered in this chapter which may appear on the chapter test. See chapter guide, warm-ups, quick reviews, and text chapter 2 parts 3-4 Organic and inorganic – how different, recognize examples The carbon atom and carbon skeleton Valence electrons, # covalent bonds Carbon chains – variety of shapes, branching, rings Hydrocarbons – carbon and hydrogen only Monomers – link in chains to form polymers Dehydration synthesis (condensation) o Joins molecules together, removes water Hydrolysis – breaks molecules apart, adds water Carbohydrates – functions - mostly energy 4 cal/gram Elements, ratio of H to O 2:1 Monosaccharides - simple (single) sugars o Glucose,fructose, galactose – isomers, all have 6 carbon atoms Disaccharides – double sugars; glucose + one other monosaccharide o Sucrose, lactose, maltose Polysaccharides – long chains of glucose molecules o Energy storage - starch in plants, and glycogen in animals o Structure – cellulose (fiber) in plants Lipids – elements CHO – no ratio, functions – concentrated energy 9 cal/gram Monomers: glycerol and fatty acid, structure of each Triglyceride – which monomers, how many of each Saturated and unsaturated – how different, where found o Hydrogenated and trans fat – what are they? Why important? Heart and blood vessel health o Atherosclerosis, angioplasty steroids – cholesterol, sex hormones, cortisone phospholipids – what are they, where found CP BIOLOGY Chapter 2 Review Name __________________ PROTEINS, ENZYMES, and NUCLEIC ACIDS These are topics and vocabulary terms for proteins, enzymes and nucleic acids. See chapter guide, warm-ups, quick reviews, and text chapter 2 parts 3-4 for additional review. Proteins – elements C H O N functions: structure, transport, defense, movement, messengers, catalysts monomer – amino acid: carbon, amino, carboxyl, H and variable (R group) R group – how many – 20; important – cross links hold 3-D shape of protein Peptide bond- covalent, between amino acids Dipeptide, polypeptide – how is a protein different? – 3-D shape Levels of structure o Primary structure – sequence of amino acids o Secondary and tertiary – coiling and folding into 3-D shape, one chain o Quaternary – two or more polypeptides together Denature – what is it? – protein unfolds; What happens? – loses function o Caused by? – temperature, pH, electrolytes (ions) Sickle cell disease – why is shape important? Enzymes –What are they? – protein catalysts Why important? – speed reactions in cells Activation energy – needed to start a reaction, enzymes make it lower Active site and substrate – what are they? Modes of enzyme action – lock-and-key, induced fit Conditions that affect enzyme action o Temperature – warm increases rate; hot denatures protein o pH – narrow range for best pH, excess H+ or OH- break 3-D bonds o concentration of enzyme or of substrate – act like a limiting reagent o inhibitors – slow enzyme action: competitive – on active site; noncompetitive – somewhere else on enzyme feedback – a product of the reaction acts as inhibitor Nucleic Acids – elements – C H O N P function DNA – store genetic information, function RNA – use DNA code to make protein what is a gene? – section on one strand of DNA, has instructions for one trait monomer – nucleotide: 3 parts- sugar, phosphate group, nitrogen base DNA and RNA - how different? o DNA double helix; RNA single strand; o DNA deoxyribose sugar; RNA ribose sugar o DNA thymine base, and adenine, cytosine, guanine; o RNA – uracil base, and ACG ATP – energy molecule, nucleotide with three phosphate groups