Which of the following is iw8(k3 piub:ox nvolved in carbon fixation during photosynthesis?

  Which of the following proteins *d,76d ,rejbz1tth1ohme a +his a hormone?

  Biomolecules have diverse formsiei; jq,e3b 2t0tm7sm and structures. Which of the following statements jmsb3i2 ;te ,t0qemi7 is false?

  Which of the following monomers can combi1 v-bgrh86dr dne to form polypeptides?

  The image shows a proteinjhnt 6p- -- ;q5wgqkak. Which level of protein structure is indicated by the letaqn;jtkw- -5g p h6-qkter P?

  Which of the following 2u kv w+ip+n q,.kim/ois a distinguishing characteristic of the quaternary structure of a proteiiu+n. v2qwk mokp,/+ in?

  Which level(s) of protein strurq eur:e he +vn-,l)h0cture would be affected by denaturation due to high temperatur,)rrhhv: neee-0uq+ les?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a resu7oq2f a:zk: lmlt of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix and a beta-pleated sxh 60jf-,c/gtzc4 -fog.f q,y,n x wsfheet? s/f.z0xx4hc -tgqjy n,-f, fow 6,cfg
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 7wuf(s:o xw t*ppo o)()z 3jcuand breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure of a p*; uh l)mqj9 umr7ns)lrotein?

  What distinguishes the tertiary structure of a protein from the secondary ssl fs4c7(n +ajuqy-u (;p o-pltructure?l(fsjl-up-4 a ;n+u7cs yoqp(

  What type of molecule is :my+qn.l p+ .e-zlnforepresented in the diagram below?

The diagram below represents the structure of the p tr x0.gfk0ht/rotein 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 formatui.+r n b7h, shqq+qo1ion 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 composition of venom samples taken from8wavz,kc , gtj2ar8k2 the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved at vw,c2rt zgj88a k,2k atemperatures 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 classifip zv35th19dli ed as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metabold 15plzt3h9iv ic 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 structuresel7kqn 3jv);w below represents the -R group in the molecule belwl); qv3jk7en ow?

1.Draw a diagram of a9e;.sli8f oan generalised amino 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) are71w:aeqn0 lu-8t owva 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 they oes47 4kysn/aplay within the body. The diagram below shows an /a4esk 4ys o7nintegral 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.