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5 Written questions

5 Matching questions

  1. Macromolecules
  2. Polysaccharides (glycans)
  3. Important Cofactors
  4. Primary
  5. Quarternary
  1. a 10s-100s of polysaccharides; storage molecules, i.e., cellulose, chitin, glycogen; linear or branched; made of similar or different subunits.
  2. b the actual sequence of the amino acids
  3. c NAD+, NADP+, FAD, Coenzyme A
  4. d m. wt. 10^3- 10^9; nucleic acids, proteins, lipids, polysaccharides. 4 most important to study.
  5. e an aggregation of two or more individual polypeptide chains; polymerase- polymeric heteromeric; hemoglobin- homomeric 4 subunits.

5 Multiple choice questions

  1. Allosteric proteins- dual affinity (hemoglobin); denaturation and re-naturation of proteins; enzymatic activity (catalysts)- apo enzyme and holo enzyme; lowering of activation energy; E+S <-> [ES]-> Product + Enzyme
  2. antiparallel orientation of complimentary strands; DNA is supercoiled in the cells; denaturation and renaturation. ssDNA absorbs more light. RNA can compete with ssDNA hybridization.
  3. CO2, H2O, NH3, N2, etc.
  4. m. wt. 100-350; nucleotides, amino acids, monosaccharides, fatty acids, glycerol
  5. occupy the active site

5 True/False questions

  1. Feedback InhibitionEnd-product allosterically inhibits the action of first enzyme in pathway. prevents cell from wasting resources.

          

  2. Enzyme Activitytemperature- denature and breaks H bonds; pH; substrate concentration; inhibitors (antibiotics) inhibit enzymatic functions

          

  3. SImple ProteinsFats or triglycerides= glycerol plus one or more fatty acids.

          

  4. Saturatedone or more double bonds (mostly between 9 and 10); Plant and animals in cold climates.

          

  5. SecondaryThe overall 3D structure of the polypeptide chain. Held together by different bonds: peptide, ionic, hydrogen, covalent, sulfhydryl, etc. Prions are proteins that don't take their correct 3D shape and are harmful; mad cow disease.