Which of the following is involved i 1x8l7jdj- + n)g4xwquexxqy3 n carbon fixation during photosynthesis?

  Which of the followib2g)n w0n lw7gng proteins is a hormone?

  Biomolecules have diverse forms and structures. Whko46td c4z) dd 6cmo5rich of the following statements is f6 5oz4t6 cor)ddk4dmcalse?

  Which of the following monirgzqypu2)87owem) r0 s6b*momers can combine to form polypeptides?

  The image shows a protein. Which level of protei q;ixcm0 l;rz(n structure is indicated by the letter (cxrqil; z0; mP?

  Which of the following is a distinguishing characteristic p/z*pl3xjm 7(ud 0wqgof the quaternary structure of a protein?dgl j0/pz 7 m(3xpu*wq

  Which level(s) of protein structure would be affected by denaturatiobuxq5 cha tto /p6:*t*n due to high temperach 5*a qb: *tott/6uxptures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of which of the following: k/g9spm7ekx2 un8 cz8
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helixg5 n c,szubn;0 and a beta-pleated sheet? 5gc, 0nnzbu;s
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 osvir6i8ny) + mf a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structuresfg rcs500u7 o of a protein?

  What distinguishes the tertiary stro m0gzm ewxk, fehr0/-4dg2/yucture of a protein from the secondary structrmwdg2o0 ygm-4x,// fehk0 e zure?

  What type of molecule is represented in the diagram5nyn -n3odtlow mj0ae aha0: rwj,9-8 below?

The diagram below represents tkuov a)nh8q3flf1 y5b* v,k)2o cdv2ahe structure 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 dip g(kqf.mka )kz/mx,p4 eptide.

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 of1odn 1/p q2/: jwcfrmg venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transport/prmofwcjqd21 n1g / :ed 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 carbohydrat-hvqe7 ks s)f xbib095es, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metabolic res f kei95sbx-7bvh)q 0actions.
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 themgm9 4( ta zhsvti:x98 molecule belosth84imxgv 99(:aztm w?

1.Draw a diagram of a generalised amino acid, and l xo) /l:1aqz+u4 tq5fk8 zdd1w gipiux ;gxg8,abel 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 foik51r alv).z sycc cw,1 +e*sor 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 influ 44r o/hmhnr/e/t9bybence the role they play within the body. The diagram below shows an integral protein in the plasma memytorm hhn4 rb/b /9e4/brane 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.