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5 Written questions

5 Matching questions

  1. hydrophobic interaction
  2. polysaccharides
  3. enzymatic
  4. saturated fatty acid
  5. triacylglycerol
  1. a a fatty acid that has no double-bonded carbon atoms so that as many hydrogen atoms as possible are bonded to the carbon skeleton
  2. b an interaction that contributes to tertiary structure; as a polypeptide folds into functional shape, amino acids with hydrophobic side chains usually end up in clusters at the core of the protein, away from water
  3. c macromolecules; polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages; serve as storage material, hydrolyzed as needed to provide sugar for cells; building material for structures that protect a cell or an organism; architecture and function are determined by sugar monomers and by positions of glycosidic linkages
  4. d the type of protein that selectively accelerates chemical reactions; example: digestive enzymes release polymers in food
  5. e a fat that consists of three fatty acids linked to one glycerol molecule; linkages that bond hydroxyl to carboxyl are called ester linkages

5 Multiple choice questions

  1. a double-stranded, helical nucleic acid molecule consisting of nucleotide monomers with a deoxyribose sugar and the nitrogenous bases adenine, guanine, cytosine, and thymine; it is capable of replicating and determining the inherited structure of a cell's proteins
  2. lipids characterized by a carbon skeleton consisting of four fused rings
  3. the shape of proteins that are roughly spherical
  4. a type of nucleic acid consisting of nucleotide monomers with a ribose sugar and nitrogenous bases adenine, cytosine, guanine, and uracil; usually single-stranded; functions in protein synthesis, gene regulation, and as the genome of some viruses
  5. organic molecules possessing both carboxyl and amino groups

5 True/False questions

  1. beta pleated sheeta secondary structure in which two or more regions of the polypeptide chain lying side by side are connected by hydrogen bonds between parts of two parallel polypeptide backbones; it makes up the core of globular proteins

          

  2. trans fatthe fat that results when unsaturated fats are synthetically converted to saturated fats to prevent the separation of lipids (margarine and peanut butter are examples); this process produces saturated fats and unsaturated fats with trans double bonds

          

  3. chaperoninsprotein molecules that assist in the proper folding of other proteins; they do not specify the final structure of a protein, instead they keep the new polypeptide separated from "bad influences" in the cytoplasmic environment while it folds

          

  4. quaternary structurethe overall protein structure that results from the gathering of polypeptide subunits; some proteins consist of 2 or more polypeptide chains combined into one macromolecule

          

  5. disulfide bridgeslinks that form where two cysteine monomers are brought together by folding of protein; covalent bonds reinforce structure