Which of the following is in3btjamwx(2jr54l + ry volved in carbon fixation during photosynthesis?

  Which of the following protei 51- e+ywp m+nooaox52zt 3aa andfs6:ns is a hormone?

  Biomolecules have diverse forms and structures. Which of 3e pc; tmv,hn ;m7pro,the following statements is fa3ehtnpmr,m o7 c;pv; ,lse?

  Which of the following monomers can combine to form polypz s/) .kiku6ppeptides?

  The image shows a protein. Which leve/p3 o-a05q,0*d5-yfs x kfqjsccz ax hl of protein structure is indicated by the letter Pck j5 f5p3szodsyaqa0/qc*h -,x-f0x?

  Which of the following is a distingui fc1 utm/-i(vsshing characteristic of the quaternary structure of c-i1/ft ms(uv a protein?

  Which level(s) of protein structure k*xy,:qhc -ax tyh7)n:q. ytvwould be affected by denaturation due to high temperatures?v tyh n.*yha qyc),kxx::tq- 7
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a resu58iw-*lc8w beeh 5edplt of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix and a beta-pq . owzgz 2w70-ijzwj3leated shee 7w-zqzzji. o0jg3 w2wt?
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 bwd8w,+6 rn8nr9oie ezreaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for vj * zm*i4m6- krg.uyybm0dn/ezm:,2q(kfscthe secondary structure of a protein?

  What distinguishes the tertiary structure of a protein from the secondaryoz hhkr8x; 7/x structho8k/ zx7h rx;ure?

  What type of molecule is represented in the diagram a;fotu:cx*/: w(nfviv .:;nq8zl faoa(ibn; below?

The diagram below represents the structure of ti4g vmnv ,b0d9t5 .hvbhe 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 q1 fx8(*d fjqtgqr4am -,ib6z 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 composls u)akx,ta/:ohj h+ + vw3lt,ition of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefa+) s ,3tx/a+vk hh u:t,ljwolully 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 beytcc xoh/9wul ubna.(, v :ayw)ct( ,/qu81po classified as carbohydrates, lipids, and protei/o t:xup./((yuu,9ah cnq,1ltow)ycca8v bwns. These molecules 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 below represent.d2o2f1j)h. mzh0. *3kc ze wvmtwpujs the -R group in the molecule below.v ww) kjmjud.mfp. z 31zc*o0he 2t2h?

1.Draw a diagram of a generalised amino acid, and label thb+ax 6ih6+jqaw0a j5y l iu31)o8dfyee 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) j64fr0zn+yoj*sd0(z mw al e -are correct 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 influencfysl9r) 0ls tm;-y) uoe the role they play within the body. The diagram below shows an integral protein in the plasma membrane of a crlt)suo9flm )0 sy;- yell.


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.