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6. In the definition of protein structures the alpha helix is defines as:
- secondary structure
- primary structure
- tertiary structure
- quaternary structure
- all of the things
7. In collagen the following AA is often hydroxylated?
- lysine
- proline
- proline and lysine
- cysteine
- tryrosine
8. Proteins have the following characteristics?
- all the things
- in some cases proteins contain a cofactor
- they consist of AAs
- the AAs are linked by peptide bonds
- proteins are sometimes referred to as polypeptides
9. In an alpha helix:
- the helical twist is always right handed
- the structure is destabilised by the presence of proline
- all of the things
- the structure is stabilised by hydrogen bonds
- the AA side chains are on the outside of the helix
10. In beta turns proline and glycine are often found at AAs:
- 1 and 2
- 1 and 4
- 2 and 3
- 2 and 4
11. In terms of protein stability, covalent bonds include?
- hydrophobic interactions
- ionic interactions
- disulphide bonds
- hydrogen bonds
- all of the above
12. The primary structure of a protein refers to the AA sequence...
- always written N to C
- always written C to N
- always written 5' to 3'
- always written as AA1, AA2 etc
13. In human myoglobin and haemoglobin the haem group
- is ligated to cysteine
- contains Mg
- contains Zn
- contains Fe
- contains Cu
14. disulphide bonds:
- are non-covalent bonds
- are characterised by two SH groups
- consist of one cystine residue
- consist of two methionine residues
- consist of two cysteine residues
15. In beta turns the following feature of proline is important
- D isomer
- cis isomer
- trans isomer
- L isomer
16. The following term refers to the addition of FA moiety to a protein
- hydroxylation
- fattylation
- acylation
- acetylation
- fatty acid formation
17. In keratin the disulphide bonds are found in
- glycine and proline AAs
- cysteine AAs
- cystine AAs
- glycine AAs
- methionine AAs
