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5 Written Questions

5 Matching Questions

  1. Gel Filtration
  2. Allosteric Inhibitor
  3. Stroma
  4. The gamma rod
  5. Early endosomes
  1. a The centrally located crank shaft found in ATP synthase thought to be involved in the conversion of an energy gradient in to elastic energy.
  2. b
    Stroma (fluid), the fluid in between grana, where carbohydrate formation reactions occur in the chloroplasts of plant cells photosynthesizing
  3. c
    This form of filtration chromatography seprarates proteins, peptides, and oligonucleotides on the basis of size. Molecules move through a bed of porous beads, diffusing into the beads to greater or lesser degrees. Smaller molecules diffuse further into the pores of the beads and therefore move through the bed more slowly, while larger molecules enter less or not at all and thus move through the bed more quickly. Both molecular weight and three-dimensional shape contribute to the degree of retention. This technique may be used for analysis of molecular size, for separations of components in a mixture, or for salt removal or buffer exchange from a preparation of macromolecules.
  4. d
    A product produced later in a catalytic pathway which inhibits the activity of enxymes earlier in the catalytic pathway.
  5. e
    This stage of endosome matures in several ways to form late endosomes.They consist of a dynamic tubular-vesicular network (vesicles up to 1 µm in diameter with connected tubules of approx. 50 nm diameter). Markers include RAB5 and RAB4, Transferrin and its receptor and EEA1. They become increasingly acidic mainly through the activity of the V-ATPase. Many molecules that are recycled are removed by concentration in the tubular regions of early endosomes. Loss of these tubules to recycling pathways means that late endosomes mostly lack tubules. They also increase in size due to the homotypic fusion of early endosomes into larger vesicles.

5 Multiple Choice Questions

  1. This process is the directed degradation (digestion) of proteins which fail to fold correctly by cellular enzymes called proteases or by intramolecular digestion.

  2. A carboxylic acid with a long unbranched aliphatic tail (chain), which is either saturated or unsaturated. Most naturally occurring fatty acids have a chain of an even number of carbon atoms, from 4 to 28. Fatty acids are usually derived from triglycerides or phospholipids. When they are not attached to other molecules, they are known as "free" fatty acids. Fatty acids are important sources of fuel because, metabolized, they yield large quantities of ATP. Many cell types can use either glucose or fatty acids for this purpose. In particular, heart and skeletal muscle prefer fatty acids. The brain cannot use fatty acids as a source of fuel; it relies on glucose or ketone bodies.

  3. Small lipid-bounded spheres which transport proteins, glyco proteins and newly synthesized lipids (which are imbedded in the sphere itself) from the endoplasmic reticulum to the Golgi Apparatus or from the Golgi apparatus to another destination. They move short distances by the process of difussion, moving long distances requires the assistance of proteins associated with microtubules.
  4. Type II fibers are white due to the absence of myoglobin and a reliance on glycolytic enzymes. These fibers are efficient for short bursts of speed and power and use both oxidative metabolism and anaerobic metabolism depending on the particular sub-type. These fibers are quicker to fatigue.

  5. Negatively charged membrane glycoprotein which help to prevent red blood cells from sticking together through the actions of sialic acid sugar which is attached to it's extracellular domain .

5 True/False Questions

  1. Irreversible InhibitorsUsually not of biological origins, these act by forming strong covalent bonds with the enzyme, poisoning them. The bond is so strong it is irreversible and example of this would be heavy metal toxicity.

          

  2. Electrochemical gradient
    The form of enzyme regulation brought about when an effector molecule binds to an enzyme at it's allosteric site, thus bringing about changes in it's conformation and therefor effecting it's ability to function. This form of regulation is immediately effective and also immediately reversible.

          

  3. Dipeptide
    This compound is one of the naturally occurring proteinogenic amino acids. Its codons are UCU, UCC, UCA, UCG, AGU and AGC. Only the L-stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. It was first obtained from silk protein, a particularly rich source, in 1865. Its name is derived from the Latin for silk, sericum.

          

  4. Malate
    Alanine (abbreviated as Ala or A)[2] is an α-amino acid with the chemical formula CH3CH(NH2)COOH. It can be synthesized from the pyruvate intermediate of the TCA cycle. The L-isomer is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. Its codons are GCU, GCC, GCA, and GCG. It is classified as a nonpolar amino acid. L-Alanine is second only to leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins.D-Alanine occurs in bacterial cell walls and in some peptide antibiotics.

          

  5. Non Competitive Inhibitor
    This form of inhibitor is very similar in structure to the substrate and can thus form an enzyme inhibitor complex which prevents the enzyme substrate complex from forming. It is theorised that the higher concentration of substrate to that of inhibitor the lower the rate of inhibitor interaction thus allowing Vmax to be obtained.

          

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