5 Written questions
5 Matching questions
- Uncompetitive Inhibition
- a Made up of repeating units of amino acids (about 20 types); Subunits linked by peptide bonds forming polymers; Function: structural support, antibodies, contractile fibers, toxins, transport.
- b The inhibitor binds to ES complex so that further reaction does not take place - either forward or backward.
- c general formula (CH2O)n; subunits linked by glycosidic bonds; poly hydroxy aldehydes or ketones and their derivatives; functions- structural support, nutrient and energy.
- d antiparallel orientation of complimentary strands; DNA is supercoiled in the cells; denaturation and renaturation. ssDNA absorbs more light. RNA can compete with ssDNA hybridization.
- e alters the topology of DNA molecules.
5 Multiple choice questions
- the actual sequence of the amino acids
- pyruvate, citrate, malate, etc.
- m. wt. 100-350; nucleotides, amino acids, monosaccharides, fatty acids, glycerol
- 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
- 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 True/False questions
Oligosaccharides → most important are disaccharides; covalent linkages of two monosaccharides with the release of H2O (glycosidic bond). i.e. sucrose, lactose, maltose, etc.
NAM → N-acetyl neuraminic acid; important sugar acids in bacterial cell walls.
precursors from the environment → amino acid with another component; glycoprotein; nucleoprotein; lipoprotein; phosphoprotein.
Macromolecules → nucleus, mitochondria, golgi bodies, chloroplasts
Ketose → glucose and glucose; glucose is a bad sugar