Which of the following is inwm 1 f6t1(znk:1fqyt qvolved in carbon fixation during photosynthesis?

  Which of the following protedvh7t0k 6voy-ins is a hormone?

  Biomolecules have diverse forms and structures. Which of the following stad.1riofv0 orl3m0 ek2knj sc /(t9 ip,tements is false?io9pid/k e.nv 0(ts1,mjok 2lf rr3c0

  Which of the following monomers can combine to form polypeptides )j pc boo)bi0vk081izgtf- z3?

  The image shows a protein. Which level of prote,pe* vw-kbre,in structure is indicated by the lbk, *revpwe,- etter P?

  Which of the following is a distinguishing characteristjf3i;/n rum *eic of the quaternary structure of a p;u e*rijf/3nmrotein?

  Which level(s) of protein s2 iryys 38m gz.e.*kzq/n8mly tructure would be affected by denaturation due to high temperatures?.*s l zynm.gi 3k rzmy828eqy/
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a re cvvfu) rhsisv5wyqc-;h*/1;m2d7 n f sult of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics d9rvu+dtnx-)dsljygo5 xh d 1i-e-33wistinguish between an alpha helix and a beta-pleated sheet? lg9ivxd5- wdhue xod31r 3sjy- n-)+t
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 xy5)nunu pa38) vc mnd0lv4p( a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following a) ccmb3 2excobj t 6f,/w**klhccounts for the secondary structure of a protein?

  What distinguishes the tertiary structure of a pr ue ar 5e9ghjd3 6tdv50y)hmq4otein from the secondary structure9eyj4u6dmhe qd)h0 t3a55grv ?

  What type of molecule is repjlup7a3gt//fw 8pc 1 iresented in the diagram below?

The diagram below re:d,kp4o* + )( fr2oactdszqarpresents the structure 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 formati tv a(n0nf oaw3rae s4-d+ x6opnc8/,ton of 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 compo4uou44m acj4 x -rec)vsition of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefu mc-u4c4eaux4 4 jo)vrlly 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 classifiedok9 sb 2z.loaew15v:a as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are thenzvsw9 a:.eo5 l ok1ab2 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 structures below represents th+b9zf)lw8vdh k,bs 2he -R group in the molecule wbsl)fh, b+9 h kv8zd2below?

1.Draw a diagram of a generalised amino acip6i.asx:kx4q;d4lmxn; xi+ f d, 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) 6:wzmoq)-hn a /q8jfp are correct 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 mq** tbvwytvsadd)j/vs27 ( :- hl)dathey play within the body. The diagram below shows an integral- tda h(*wbvt va2lm/7:ds*s)j)vydq protein in the plasma membrane of 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.