Test yourself: 2

EU name: EXINT2

 (Date: Aug 24 2016 EXINT2 )

This page contains a randomly selected series of exam questions that we have used in the past in real exams, and that you should be able to answer by now.

You find all these questions again in the ′Test-exams′ section, and in that section, you often also find the answers.

Exam questions used in the past:

  1. Which residues are hydrophobic?
  2. Which residues are hydrophilic?
  3. What is special about proline?
  4. What is special about histidine?
  5. Why is Proline often observed at the surface of a protein?
  6. Why is Tryptophan the most conserved residue?
  7. Align without gaps and explain your reasoning:
    LLLDAWLLL with LLLDWLLL
  8. Given a pattern definition from the PROSITE database: -G-[AS]-x-{RHK}-x3-C-
    Does the following sequence fulfill the pattern? Explain why (not).
    GASRLKSC
  9. Why are Asp, Asn and Ser more often than other residues found in beta turns?
  10. Mention two types of mutations (i.e. Phe -> Asp or Trp -> Ala) that generally make proteins more stable (perhaps this question can only be answered in two weeks...)
  11. Why is Leucine not a good active site residue?
  12. Why is Cysteine seldom seen at the surface of a protein?
  13. Why is Proline often observed at the surface of a protein?
  14. What is helix capping?
  15. Which residues are good for a helix? And why?
  16. Why is the capping effect by charged amino acids stronger at the N-terminal end than at the C-terminal end of a helix?
  17. At which end of a helix can you find prolines, and why?