Which of the following is involved in carbon fixation during photosynthesisc8 qiu8 t82u(vifm,kb?

  Which of the following protei z8 gc1upaf:m8ns is a hormone?

  Biomolecules have diverse forms and structures. Which ahmg9bd gc+7, fl(t8sof the following statements gt+7, b mlhc (8a9dsgfis false?

  Which of the following monomers can combine to f2-r nyx blop 3 v;3x5(kf2vm,ufckny4 orm polypeptides?

  The image shows a protein. Which;sp;fcc3j- +3i a1z j-xgmct b level of protein structure is indicated by the lpb -+;stz3cmxjgi f1cac; 3-jetter P?

  Which of the following is a distinguishinnre0 (o *8jolde9*aweg characteristic of the quaternary structure of a pro9a8eo( l*rdne*e 0wj otein?

  Which level(s) of prote h c jqfhggxaue/(.5c ru8922fo71 pbqin structure would be affected by denaturation due to highf( uu12fgx58p 2rhj bq.cq7hog /aec9 temperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a5/g3l7g rl :karr+qqm result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix and a beta-pleatx- vsje47ne 6t:p2viq z arv8:ed sheexraezv 7ei :46p:t2sjqn v 8-vt?
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 andm yun(3hkd 2e4 breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structupbti88 qeof*nlr-g:- re of a protein?

  What distinguishes the tertiary l 5gtrtxh29up (2jzzxv7v) 6d structure of a protein from the secondary structu tuxdp6z9 vxl(2g7v) 2h jrtz5re?

  What type of molecul : ymcb13j:itit( u t7c3z2unie is represented in the diagram below?

The diagram below represents the structure of the protein haemo/ :gv5:bl5+sx n)r wud (vb3mmzwrin9globin.


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 dipe mx*6 vc: *v5rjhkfz7uptide.

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 compo95p2km ieg( ouq2ui2w wv 6x0csition of venom samples taken from the Malayan Krait (B. candidus) found in three localities;2p uxwiemq9wiko v u0c6 (252g 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 metabolism cacy4ccu/ m+ y7en be classified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metabc 7/4cye +mycuolic 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 rfqft9d+ z s:ih7zhg.5epresents the -R group in the molecule b+d 7gf9hz5 sft.:h qzielow?

1.Draw a diagram of a generalised amino acx6cmk que hlu:97zd04id, 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 for amino acmtmf4ah :9r.o, g3ob1t f1zeyid 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 influenceiy/k ws3v3nu /sph9fm9nqe+dc/,4ym the role they play within the body. The diagram below9d+i//cyeyqmnf34 s9u h/k 3wp vsmn, 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.