Which of the following is involved in carbon fixc:/ye g6m(g 4v/czxc xation during photosynthesis?

  Which of the following proteins is a hormonmu+a.e 6wk..(uy o;lm okmbw5 e?

  Biomolecules have diverse forms a+vknde:9-w q end structures. Which of the following statements is false?enkv ed-q9:+w

  Which of the following )2(qdwsejb q0 monomers can combine to form polypeptides?

  The image shows a protein. Which level of protein structure is iiad1m iz 5n*dr 68)gy.i deo1xndicated by the letterid e 61i5ox1ydgzdn*m8 ) .ari P?

  Which of the following is a distinguishing characteristic of the quaternary stra7wirbg8m/zz945ew nvqs-w /ucture of a pw94i raq//m7g bsv-zzn5 8wewrotein?

  Which level(s) of protein structure would be af;p9. rq uhtp.bg*o cp:*m3 gmofected by denaturation due to high temperature;q*g.pm: pmbho3pu r g.t9*cos?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is ;2pl c)zt vw1t uf/kp)a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics dis +dewc d*mcvv* m.t qw7:7*trytinguish between an alpha helix and a beta-pleated sheet ce+qdmmwd7cv:. y*t*7r w*vt ?
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 dojr0lu 391 mvghwn of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accoun 02cfi0,8qqu - cmkqopts for the secondary structure of a protein?

  What distinguishes the tertiary structure ofv tai+c,4pol8yuoh q w8p*d;e/ o2f.x a protein from the secondary structu yp;h qp+ui28xd.owo*a/e4to8v,lcf re?

  What type of molecule is represj 9 x/b:5itxtggcnjl17bi (7yented in the diagram below?

The diagram below represents the structurd u:wq hyl v38 -cs5n- 1v3gycbw-k:wre 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 formation of a dipeptic2j zmt.-zcvxpn11bpgkp8 qh8g(w( 2de.

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 thh6cn,dhjskz e1mz 3a(/6vs h/ e Malayan Krait (B. candidus) fo,/damhj6/(1hh63szs zv ecknund in three localities; 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 bec-v ;xbu,p dd7/-huc6 lls,dn classified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units lb n 7p--x,cdv,u s dd;hlc6/uwhich 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 n3a9 f vd.2lj ;t (j:bfan,kddbelow represents the -R group in the molecule belowvn2:jdn ld,3af9a(bdfj ;t.k ?

1.Draw a diagram of a generalised amino acid, and label the functional groupdy:uorlj7 ,/ as.

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 co fh7ff q0a3h67ft:aifrrect 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 bo53 s;6yvrx h rqtjb8+bdy. The diagram below shows an integral protein in the plasma memb;xr+ q5hrvj63sbt yb8rane 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.