Which of the following is i4xj )yj :)foe,(bl dlynvolved in carbon fixation during photosynthesis?

  Which of the following proteins yvt7zel mr u3v8 8ie4+is a hormone?

  Biomolecules have diverse forms and structures. Which of uf.) i4 ifz:jbthe following statementu.i4 :jff)ib zs is false?

  Which of the following monomers t-:8 rl*qe pldcan combine to form polypeptides?

  The image shows a protein. Which level of protein s1 e)zdnszu3+ftructure is indicated by the lu3)+d nszf z1eetter P?

  Which of the following is a distinguishing b ea5 q,k- ijv(0f*ydecharacteristic of the quaternary structure of a prot-ki 0jb*v(ae, 5efdqyein?

  Which level(s) of protein structure would be affect)7nsc lyd q:f 6suj1z+mg5pu5rdr8q ) 4y 0lpped by denaturation due to high temperatures?m s1g y)lzr:74d6uyp u0ndj5s)r+lqq8f5 p cp
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structuhm/ )dd m3wh.9 pu5-vlt73cm6ndk loyre of a protein is a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguishx)yb ,6fl2jsr6 , fkst between an alpha helix and a beta-pleated sheet? ,6btklxy fs2)jr6s f,
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 polym4y,2d)edrju jh z)fj)er.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the seco9 7pbejoyw// yndary structure of a protein?

  What distinguishes the tertiary structum zd.2ew64 :c 1qiiwbqre of a protein from the secondary structure?i4 z 6m: i12.ewqwdcqb

  What type of molecule is represented in pnnp.waxyr48y( mt7k ;zke7 l1 ir9z. the diagram below?

The diagram below represents the sdv bqxx*)k ./d3 x- srjh9t z-q9siwf0tructure 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 formarou2 p57m 8u6q0onyumtion 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 tbu3d7jf;w6d j aken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved at d6dwf jb;37 jutemperatures 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 catd 9 8ye**axgen be classified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved i 8x**9dtagee yn 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 the molen5(b57wqqke t:tkvee2ev1 pu- +h.r g cule v-eguq 5e.7tkrkq te2bw p+(5e:h v1nbelow?

1.Draw a diagram of a generalised amino acid, and label the functional groups. 14fqm+*fkdfw ;2(i ilmjy 6ak

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 followingi v0t r41iq i3 ys16 m8g5kp(alsryo;g statement(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 inf(m +exrhk9-qwluence the role they play within the body. The diagram below shows an integral protein in the plasma membrane of a cemw -e+(r9h qxkll.


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.