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5 Written Questions

5 Matching Questions

  1. Macromolecules
  2. Enzymes
  3. Polysaccharides (glycans)
  4. Secondary
  5. Activation Energy
  1. a Usually polymers; usually dehydration synthesis also called condensation rxn.
  2. b Needed to disrupt electronic configurations; physiological temperature and pressure too low for most chemical reactions to take place. Enzymes serve to speed up reactions by lowering activation energy.
  3. c 10s-100s of polysaccharides; storage molecules, i.e., cellulose, chitin, glycogen; linear or branched; made of similar or different subunits.
  4. d Biological catalysts- specific for a chemical reaction; not used up in that reaction; Apoenzyme: protein.
    Co-factor: non-protein component; Coenzyme- organic cofactor (NAD, FAD); Holoenzyme-Apoenzyme + cofactor.
  5. e The localized twisting and folding of the polypeptide chain. A specific orientation in space. Two main types: the alpha helix and the beta sheet. Helix- parallel some of the strongest; alpha keratin-nails; spiderwebs. Pleated sheet- anti-parallel; Beta keratin- silk. 18% of all proteins are one of these two shapes; others are random coiling

5 Multiple Choice Questions

  1. Fats or triglycerides= glycerol plus one or more fatty acids.
  2. all hydrocarbons have CH2 units (bad for health); animals
  3. m. wt. 10^3- 10^9; nucleic acids, proteins, lipids, polysaccharides. 4 most important to study.
  4. N-acetyl neuraminic acid; important sugar acids in bacterial cell walls.
  5. general formula (CH2O)n; subunits linked by glycosidic bonds; poly hydroxy aldehydes or ketones and their derivatives; functions- structural support, nutrient and energy.

5 True/False Questions

  1. Hybridizationcan be done with RNA or ssDNA

          

  2. Oligosaccharides+NH3-CHR-COO-; dipolar charges neutralize each other; side chain determines the charge. Carboxylic group and amino group form the peptide bond (H2O leaves). Peptide glycosidic bonds most important; 150 in our body only 20 make proteins. you have 3AA that make a tripeptide 3^3= 27 different combinations. more than 200 AA in a protein on average.

          

  3. Unsaturatedall hydrocarbons have CH2 units (bad for health); animals

          

  4. Noncompetitive or Allosteric Inhibitionoccupy another site on the enzyme, altering the active site.

          

  5. Important Cofactors+NH3-CHR-COO-; dipolar charges neutralize each other; side chain determines the charge. Carboxylic group and amino group form the peptide bond (H2O leaves). Peptide glycosidic bonds most important; 150 in our body only 20 make proteins. you have 3AA that make a tripeptide 3^3= 27 different combinations. more than 200 AA in a protein on average.

          

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