Which of the following is id.fvwao1sjsav3ggg ul :k(32 k +9t )mnvolved in carbon fixation during photosynthesis?

  Which of the following pz;ch (u1hpm76 4mrqwjroteins is a hormone?

  Biomolecules have diverse forms and structures. Which of the followi+pkw.ka6- czt ng statements is falsezp6k+a .kct -w?

  Which of the following monomers can combine to form polz,d .loufs dlx3oc m;-ej:( .jypeptides?

  The image shows a protein. Which level of protein structure iszg11szh*9j rr9ar ;t vw0lq w6 indicated by the lvr 1st09q w9harlz1 ;gzw6r *jetter P?

  Which of the following is a distinguishing chwv36ev)l +p )ng rcn7,h,hiyn aracteristic of the quaternary structure of a proteihivn3lhwc7 ,ng6+ pny),) vern?

  Which level(s) of protein structure would be affected by denaturrpx;*;dhb d(oation due to high temperatures? o (*;d;xpbhd r
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of which of thes;cgm6 i89 tjv following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distiplerlf99ra yph x3nee; d3v0m7d:q8;nguish between an alpha helix and a beta-pleated sheet?9rx:3 ;fqr v;p3ml 8 eph0eade7ynd9l
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 breakinj.tx5i q2gk k-g down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the s )hqv1/ a-nbfk a232sgauk,doecondary structure of a protein?

  What distinguishes the tertiary structure of r2ezd)nt1dvy2h+ 0gdah. /fpa protein from the secondary structu g/1+ nd)y z2.rveah0h2fpt ddre?

  What type of molecule*gmd+. ;jc4fu 8boky l is represented in the diagram below?

The diagram below represents the strup3t5dlmsibq/: .s4z8r,i g ya cture 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; 3.sg5;6di6mf8vcx y39iirccc cne x 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 ons5yuo 45,-hjanu 5zh:zpa ): oxe6zkr the protein composition of venom samples taken from the Malayanzo )rka55: oyhz-6pnxaszj e5u :,h4u Krait (B. candidus) found 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 metaboyvrs40pp)k;dw o6fd (lism can be classified as carbohydrates, lipids, and proteins. These moleculesr;o(p v4 k)fd0dsywp6 are often broken down 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 structures bel8suxv:qpse5l c0/g*t ow represents the -R group in the molecule be8q eugtx* c0/spl sv5:low?

1.Draw a diagram of a gu ztqx4jll (7c5n0 ju;eneralised 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 correc hyv -rm7bbi13g ft)j- a9jhx)t 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 infl2xttc3;(nikww;k e, luence the role they play within the body. The diagram below shows an integral protein in the plasma mck wxln it;ekt32(,w;embrane 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.