Which of the following is invgg:j2 pr evk vxk)/t-2n2 k0maolved in carbon fixation during photosynthesis?

  Which of the following proteins is t g-;eko6 nhnny-fui0n4/fv; w/i*aba hormone?

  Biomolecules have diverse forms an5rrxqy4j5dq2 ,+nw5ngz qh .fd structures. Which of the following statements is falf+nrz yg,5rqq wdj 55h.q 42nxse?

  Which of the following monomers can combeb-ouv f-1rt2en)-ol,e z g :r5tp)ge ine to form polypeptides?

  The image shows a protfu4zb kj-3 qsnqj*-v 9ein. Which level of protein structure is indicated by the leujqbn -q9zj4-*fs kv 3tter P?

  Which of the following is a 2je :l.lfy l)zjkis1a akz5 gev5;2o 5distinguishing characteristic of the quaternary structure of a proteae: 2.lg ko ij5)5slvyzjle; 2fzk15ain?

  Which level(s) of protein structure would be affected by denm m qeb)ph+26haturation due to high teem2 mb)+hhq p6mperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of which oo(abfo019t gt*oa :em3ir0hk f the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distintv4blk(d 2y,yguish between an alpha helix and a beta-pleated sheey(ykb,4v2 ldtt?
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 breakdvdiju9p wxd o,s ,hy5-a .8h;ing down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the send:/ kwqcx0vnkbd* 4gz2s6e 2condary structure of a protein?

  What distinguishes the tertiary structure of a protoc c x6kw)v:vojs0 ,.mi(ha,tp /vad2ein from the secondary structura v,cjikv.:d(o 2ma/sc tpx6o0v,w) he?

  What type of molecule is represented in thukppn1 j -s q-t ue3lr g*wj8qcfmio +/9)1f7fe diagram below?

The diagram below represents the structure of the protein haemoglobinx,o n63kht 7rp.


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 ;2a r y +4schihqc30ttof 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 from the Mapmz 9gn0 mic:)layan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved at temperatures bm9pc : m0)ingzelow 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 classifiedp+;/ )quuozv sh+ls:i as carbohydrates, lipids, and proteins. These molecules are often broken do/vl) usip o qsu+h:z+;wn 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 st,,vhi*br50c/i kuyzr ructures below represents the -R group in the molecule below?k bv5y rcizu/,*irh, 0

1.Draw a diagram of a generalisedhd5i+s7k gs ab/z7m/ jv8gn 0c 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 statemea. 912d jgqwcent(s) 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 they play within the body. Th. o*nsa f2va-fe diagram below shows an in2o -ffv *nsaa.tegral 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.