Which of the following is involved in carbon fixation during photosynk0qbumsxbkg91 hu*ai3gh -;gz :xdo, z/)b9ythesis?

  Which of the following proteins is a h(s,yimrqynf.e ) ,v:de 5,atcormone?

  Biomolecules have diverse forms and structures. Which of the following statemen(53rhk4b xaq2ngc8 xatsx ak8n3h (cg25b4qa xr is false?

  Which of the following monomers can combine to fom+ idvyttb5w4.u,gp4 rm polypeptides?

  The image shows a protein. Which level of protein structure is indicate;glxkv81grqivz7 54ed by the 58kqgv;g 4eirl7 xz v1letter P?

  Which of the following is a distinguishing characteristic of the quaternary7 fzs(dvci(y* structur(yszi*(dvf c7 e of a protein?

  Which level(s) of protein strucm5 ,f j5h;pvgmture would be affected by denaturation due to high temperatur5 ;mj5pv, fgmhes?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure mpiioppdm 24.b/:xkx(r+:xq of a protein is a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish betweenoksgn42b;fyl86 zkocd:pnl//s (2b d an alpha helix and a beta-pleated sheet? slyfl 2z2bo8bkn ;/g4pd6s /n (okc :d
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 forlli yy z0mc+cxb6eyv,57r 3 e.mation and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure of a protein? 8x* o5k*pn( fpa1.icy)0mruohp0 fym

  What distinguishes the tertiary structure of a protein from the sech9 1rmnq44g a qx hgmzi0;e;j/ondary structure1gxirmhjgq49; 0 ma;he/4zqn?

  What type of molecule is represenlggd2 j.z k4s5ted in the diagram below?

The diagram below represents the structure of the protein hamnge y*30 h-on4c)(boy zeo/ hc+na7iemoglobin.


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 forma4r.xe(blymaocaxk)0 4 9bm 8k i5:sf ztion 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 tak/ u lkr-84)1iyj mtzsden from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved at temperatures bel 1)d-it48mlur/skjyz ow 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 carbohydrates, lipg30br,j wmn7m 33 chlpids, and proteins. These molecules are often broken down into simpler units wh0 h3w 3rl m7b3c,mngjpich 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 represents the -R group in the molecules)0 n6xeg/ dkghr :r0ek)dz3 d below?3d /60zksg) r kh0 drdxn:ge)e

1.Draw a diagram of a gg68o1t1uht)o yvk: o- py(js+vj2.iun x h kr2eneralised 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) are cor 8uj 12zui.j/y q*kmlffek .6trect 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 wit).q 2fh8cm . 2prnqmtghin the body. The diagram below showc.pqn 8)t2fmrqmg2.h s an integral 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.