Which of the followi5iki/ arm k7g+ng is involved in carbon fixation during photosynthesis?

  Which of the following pr3ct vw 7(oxz9qoteins is a hormone?

  Biomolecules have diverse forjjihun9 nq:x 5 qprjh-; (;2spms and structures. Which of the following statements ipu- ps j2x;njn;(hqij:r5q9h s false?

  Which of the following monomers cc4fba46 fppiip3,k)pq (qnf+an combine to form polypeptides?

  The image shows a protein. Which level of protein structure is indyc9xm 8;crp3w,ac o:xb-k -sz icated by the letter crwox8-b ak x;zsp9,c3y:m c -P?

  Which of the following is a distinguishing characteristic of the qua75ax4l,2.wpwyj -ku j5h cqjq ternary struc pujw.qqc7 l,j2a 4w55xj khy-ture of a protein?

  Which level(s) of protein structure would be affected by denar0so a ,9nq 5k7 z b+8r6wom2zshpo*katuration due to high + ,qb 2k aor9no 8m5zosh6*r s0zkaw7ptemperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of whic(ac )-ao-.l,xhxyv q dh of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix and a b3i1p6rfpl m(5 is qp.yeta-pleated sheeii5mqrp 3p 1p6ys(lf. 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 a polymer. qofd fcicsz3kl0 u:2 e o+:83c

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the followi1faq maw)p :4gng accounts for the secondary structure of a protein?

  What distinguishes the tertiary structure of a protein from the sm:y(ry,cf x2 ebc3t g*econdary structurg*y m 3, y2b:fertc(cxe?

  What type of molecule is represente10n19cl(dang.c3v k+f rjnm ed in the diagram below?

The diagram below represents the structure of the protein haemoglobin. 9:2( fwb1bi8emsxqri


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 a nqfmnhyx791 ,za;r( ddipeptide.

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 taken7 eupn.*6 uf8gzld q3d from the Malayan Krait (B. candidus) found in three localit*lzf3e dun8d.6qpu g7ies; Malaysia, 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 carbohydratk/.p) z iq x.u9eav+fmes, lipids, and proteins. These molecules are often b zv/ea)uqi+fm xpk. .9roken 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 structures below represents the -R group in theehahi)0kk b 53 molecule below?)ikhh 53 ae0kb

1.Draw a diagram of a generalised amino acid, and label the funcra7 df-s 7 -p-kly5bhyzi(o5r tional 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 correct for ami ,u ncl+4h0olqdm33oi 99sxibr 8)rve no 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 bo+9 i ,icgnnr-:xzlrlda.e (. mdy. The diagram below shows a inizlre. (al.d-+ gc9n,mxr: n integral 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.