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5 Written questions

5 Matching questions

  1. Hydrophillic residues/amino acid
  2. Caveolin
  3. Exocytosis
  4. MItochondrian
  5. Membrane Biogenesis
  1. a
    Sausage shaped organelles with a double membrane. The inner membrane folds in to cristae. This organelle plays a fundamental role in the production of ATP in eukarayote cells and they are abundant in cells which require high amounts of energy such as muscle cells.
  2. b The production of new membrane material, whic takes place in the ER.
  3. c A transmembrane protein responsible for the formation of caveola.
  4. d
    The process by which substances are exported from a cell.
  5. e Amino acids which are polar and are attracted to water examples are Glutamine, Serine,Theronine, Histodine, Lysine. Hydrophbicity is also affected by pH levels in some cases.

5 Multiple choice questions

  1. The carbon bonded to the carboxyl group in an amino acid.
  2. A short polymer of 2 to twenty nucleotides. Derived from the Greek word Oligo, meaning few or little.

  3. Organelles that are plentiful in liver cells and adipocytes, responsible for breaking down fatty acids and amino acids in to hydrogen peroxide (among other things) via the action of an enzyme known as catalayse.

  4. Membrane lined gap junctions which cross cell walls in plants.

  5. A small regulatory protein that has been found in almost all tissues (ubiquitously) of eukaryotic organisms. Among other functions, it directs protein recycling.It can be attached to proteins and label them for destruction. This protein tag directs proteins to the proteasome, which is a large protein complex in the cell that degrades and recycles unneeded proteins. This discovery won the Nobel Prize for chemistry in 2004.
    The tags can also direct proteins to other locations in the cell, where they control other protein and cell mechanisms.

5 True/False questions

  1. Endoplasmic Reticulum
    Cell organelle responsible for synthesizing proteins.


  2. Substrate-level phosphorylation
    The process of synthesizing amino acids based on the genetic DNA code, this involve ribosomes which are a complex of several RNA molecule and up to 50 proteins. The ribosome decodes the anti codon of the tTNA to the codon of the mRNA.


  3. Cadherin
    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.


  4. Catalytic site
    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.


  5. Heterochromatin
    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 .