Which of the following is involved in 7;0hebq m, dg2 0jhccscarbon fixation during photosynthesis?

  Which of the following pro1 eb:38w vano) blwnh27hx;wtteins is a hormone?

  Biomolecules have diverse forms and structu k.hn5sm6byw4or o7z-res. Which of the following statements is fals z 5. nbyoso-7hmw6r4ke?

  Which of the following monoylm.e d eew0j:m+h)c 6mers can combine to form polypeptides?

  The image shows a protein. Which level of pmu (a(kl(g7 +4wvxh 97iwg,my au4hmfrotein structure is indicated by the lettg7v 7 (ku m9ulaxf+,(iyha g(mw4mhw4er P?

  Which of the following is a distinguishing characteristi ao0al q )*6aj9w06irf itzvw5c of the quaternary structure of a pr jvaqa6az* tor9w0i )5fw 60ilotein?

  Which level(s) of protein strusve(-myg:m3 l8yhop7+ 7eve t cture would be affected by denaturation due to high temp 8y om7lv -v7+e(ytg3 sep:hemeratures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of which of 3xxg280 auidq:n)htkthe following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha: sn5w6tx v 12 )z:dlwidwlm*h helix and a beta-pleated shee2:zi* : m5nwwd6lx)wht d1sl vt?
I. The positions of hydrogen bonds between different amino acids
II. The location of hydrophobic interactions between nonpolar R groups
III. The positions of disulfide bridges between cysteine residues

1.Distinguish between the formation and breaking down of a9b *+.2ee mqtfpo u.bi polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure f9wk 3jqun zv5o4kfs44 x*l p3of a protein?

  What distinguishes the tertil 5t-nr;- rm p9f4b6gl7lixxmary structure of a protein from the secondary structur5f4n- 9x -m i7rxrtl6;mllpgbe?

  What type of molecule is representedq ur8/; )vc.uyb*gqzq in the diagram below?

The diagram below represents the structugn3w pu/:i0 vure of the protein haemoglobin.


1.1.State the function of haemoglobin.

1.2.Describe the structural differences that distinguish one protein from another.

2.Haemoglobin is part of an organism’s proteome. Define proteome.

3.Describe how the structure of a named protein, other than haemoglobin, is related to its function.

4.1.Explain the impact high temperatures can have on the structure and function of proteins such as haemoglobin.

4.2.State another abiotic factor which can impact the structure of a protein.

1.Describe the formation of n0; lkr1mfbuss- aezc9;( +zcqri q-2 a dipeptide.

2.Explain the impact of one extreme abiotic condition on the structure and function of a named protein.

3.Using named examples, outline the variety of functions found amongst proteins.

Data was collected on the protein composition of venom samples taken fry;e lcazz/- 3gom the Malayan Krait (B. candidus) found in three localities; Ma alzyze ;3/-cglaysia, Indonesia and Thailand. All samples were carefully transported and preserved at temperatures below 20$^{circ}$C. The graph shows the number of different types of protein found in each venom sample.


1.1.Identify the independent and dependent variables in this investigation.

1.2.Venom samples were collected from different snakes, in different localities. Suggest two controlled variables, other than temperature, that would support the collection of comparable samples.
Below are the results from gel electrophoresis of one group of venom proteins.


2.1.Identify the group of venom proteins shown.
2.2.Explain how proteins are separated using gel electrophoresis.
Different mice were envenomed with samples from each of the three localities. It was observed that the venom with the lowest neurotoxicity was from the Malayan krait sampled in Malaysia.
3.Suggest why it was important to transport venom samples at temperatures below 20$^{circ}$C.
4.List two advantages of using mice as model organisms for humans.
The venom samples were further analysed, and it was suggested that the Three Finger Toxins group (3FTx) of proteins contributed significantly to the neurotoxicity of the venom. This prompted a closer analysis of the different types of 3FTx proteins found in each venom sample. The data was presented in a graph.


5.Based on the data, suggest which type of 3FTx protein is most likely responsible for differences in the levels of toxicity observed between the different venom samples. Justify your answer.

Molecules used in metabolism can be classified as carbohydrates, lipids, and i7h9uuxc(qppxb00 d ;5o+ vgf proteins. These molecules are ox0 ; v(po i5ugq0+97fucx hdbpften broken down into simpler units which are then involved in different metabolic reactions.
1.Identify two disaccharides and the monomers from which they are formed.
2.Draw a labeled molecular diagram to show a generalized amino acid.
3.Discuss the theory of vitalism and its falsification.

  Which of the following strucm 8g sv(8(s,; cjiyk0qoua,betures below represents the -R group in the molecule belbjm(8c o ,,sie gyvs(k;q0au8ow?

1.Draw a diagram of a generalised cg.5cw+ nlio*2 *bnexamino acid, and label the functional groups.

2.Outline how a dipeptide is formed.

3.Explain how extreme pH and extreme temperature affect the structure and function of proteins.

  Which of the following statement(s) are cormyks vsg ,3g, bk7h97jrect for amino acid R-groups?
I. R-groups can be hydrophobic or hydrophilic.
II. Hydrophobic R-groups are polar.
III. Hydrophilic R-groups can be acidic or basic.

The properties of proteins influence the role they play within the body. The d;1f 0xj-gu. m squvk7siagram below shows an integral protein in the plasma membrane o0fjs7vu-.qgs ;kx1u m f a cell.


1.1.Describe the influence of polarity on the position of amino acids within integral proteins.
1.2.Other than polarity, state another chemical property of amino acids that can vary due to charge.
2.Using named examples, distinguish between conjugated and non-conjugated proteins.
3.Outline the role of interactions and bonding in the determination of protein 3D structure.