Which of the following is involved in carbon fixation during photosynthxqm j2ug)+p gw r+n5p;esis?

  Which of the following prjetn;dpu /m9czo3c 7 8oteins is a hormone?

  Biomolecules have diverse forms and structures. Which oflhmxpl8 x*(fa sf )6kf8vdr:2 the following statements is false?xxl:hpvadfk6 fl) 28srfm8*(

  Which of the following monomers can combine to form polypeptidesa xnxgz.e qq) w8 q3iydq9y:ne1q3y;-* mfwp9?

  The image shows a protein. Which level of protein q6x f ck.bbg36structure is indicated by the lettf6cb.6b g xq3ker P?

  Which of the following is a distinguishing characteristic of the quaternary s3 4dtg5e04f yh4a nizbtructure of a protein?td3nz4a5 y4 0fgei 4hb

  Which level(s) of protein structure woutg e(+- tz fpwx5b:gid :n:je6ld be affected by denaturation due to hig b6dg wxz5- (fe +jenpt:t:g:ih temperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protei hk1 woi+3ak6ifo0n d0n is a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix and a betatz9cz z3d3rml(r gv.el2lk5--pleated sheet?rlclkzl gz (3m- vd5t.rez 239
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 po3 p/:evpexs t6lymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts forfut ao+,3f +sb the secondary structure of a protein?

  What distinguishes tha*u .99 pkk p zo,yoaba)mwy5y22bs5ee tertiary structure of a protein from the secondary structurea929 o)ku.be5 *ay kp, mwybps52aoyz?

  What type of molecule is represented in the diagram belowt*:cn2pukv+umnhmf/llpf l33l 7e0h(k+h a* ?

The diagram below represents the structure of the protein haemoglobin. hfj93(b7 d4 bru2kasz


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 format00iy f/oajoe5 ion 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 ven)rek0k wzb/+fom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and r0b k )zwk/+feThailand. 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 puisn37rri 71 classified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metabolic reac7 spi7r1 3rniutions.
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 followi:aw4z5ztk ynec7;8 hg 6bgqh8ng structures below represents the -R group in the molecule belzy6kgwcq88 :a7; bhz n h45tegow?

1.Draw a diagram of a generalised amino acd3f(xz2, j ap*ux9b g2dhs9v sid, 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 correct f9m2bk zo 2bys+hzs 1w-or 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 pl7m;r22i -. mlj df.szk8sxbad t92g q,wwth n7ay within the body. The diam -t.nzd ajh ;kd72.sx2l f2w8gwrqms,t9b7igram below shows 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.