Which of the following is involved in carbon fixation durix04ispzb/ 0jgxw/ k9 y,oi )teng photosynthesis?

  Which of the following proteins is a horm o9w6*memt7m vone?

  Biomolecules have diverse forms and structures. Which of the following staxh+d1 dl2 dxg8tements hdxl1 8 2+xddgis false?

  Which of the following monomers can combine to form polypepqq*i x8a,deodsi3zwi 7 (t35ptides?

  The image shows a protein. Which level of protein structure istwph34 as(* za qoc- 1ahgn9c:7gt,hy indicated by the leth*-c 3,9op ghth4zsy(a7cat1qa ng : wter P?

  Which of the following is a distinguishing characteristin :fw5rj-1j;r-wecsxc of the quaternary structure ofjs1refx: c n-rw-w;j 5 a protein?

  Which level(s) of protein structure would be affeccve b0gtxw3 4dpf46t/ted by denaturation due to highc/t gv4d0fpbte x 6w34 temperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result o c9*xn(8j-nt hm q7 frfasl6v.f which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between hh2c,t4 ; 3gb9vwibbjan alpha helix and a beta-pleated sheet?3wh9bjh g i4cbtv;,2 b
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 d j*7vexi5qn-z own of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secodguib q;4,-h .u sa,nvndary structure of a protein?

  What distinguishes the tertiary structure of a protein from the secondaodv -aksps- 9iqm nzkii c40 :6v7g+u2ry structure?0 mk7sizpq492gk-:vai o i-vu6 scnd+

  What type of molecule is represented in the diagra)9o1qs qhfpjh3k )*f c**qbkgm below?

The diagram below represents the structure of the protein haniu ( 202qu ypf9x6edbemoglobin.


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 dipe5d5 5)wxdzg viptide.

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 My,*mm )v;dy qa2e0b6r *fumol alayan Krait (B. candidus) found ;fqel0,yo* 6urdmm b)y*va2 min 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 be classified as ca/rccvpb.) / g(kto n9nrbohydrates, lipids, and proteins. These molecules are often broken down into simpler /cnnocbp)(gt /rkv. 9units 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 reprm ds6q41m72bb-fj qk: o hx.znesents the -R group in the molecule bh:mbn4 x.f2 -jq1mkqozs67b d elow?

1.Draw a diagram of a generalised amino acid, and label the functional gro dgh m:n:;,ur*:s rbvoups.

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 k58peuiy)z6h o 4-zd acorrect 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 plq in/c( vog57yay within the body. The diagram below shows an integral protein in the plasma membr5gi /n7coyv(q ane 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.