Which of the following is involved in carbon fixation during photosynthesl-b4bn2d 4t6c rjxut9is?

  Which of the following proteins i; p ;uj plhn l8zsj-9xb9).n/khdipl. s a hormone?

  Biomolecules have diverse forms and structures. Which of thn ionbeli14m)s . ks e1:,ur*le following statement ir b lnks*en, :s1em).14louis is false?

  Which of the following monomers can combine to form polypeptides? key .x;op yd2k3a 5orauf()0l

  The image shows a protein. Which level of protein structure is indicated by t,7o2 hf9htagohe letter P? 2oa9th, go7fh

  Which of the following is a distinguishing n/ii,etj njt/db5 e30 characteristic of the quaternary structure of a bi 3//j0e5 enn ,itjdtprotein?

  Which level(s) of protein s itsm2(np*u: k(nb w+bay-at)tructure would be affected by denaturation due to high temperatu:(ta u2 n-i smtw*yn+pb) ka(bres?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of k(- 1mq0tgwe jwhich of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix and agub-2bg wu8/5lbnmi 1 .y w/cy beta-pleated sheet? 8mgib w15b-g yyw/2. lnu bcu/
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 formati tg pyfgw2-.g2/vdn g r-9j.roon and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure of)rde9i) psv+a a protein?

  What distinguishes the tertiary strzmzq v8(-78t ed bk4apt)ak a:8 n/kmhucture of a protein from the secondary structur a: b/za(eth78 pv)d4 8k-tmakk8mnq ze?

  What type of molecule is representkczt:phw1q 8 9ed in the diagram below?

The diagram below re5d51ht jj 2,-yofhedjv qk,1 dpresents the 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 dipeptim :x: .j,/rrpr8wt8 x jdzjjq)de.

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 venom samplay v.j4(p 7tqzes taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved at temperatures below 20av.y74q j zp(t$^{circ}$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 carbohydrates, lipidse 7sxg y94zlv/3i8 velpn*b y(, and proteins. n gv3pz94lx7e8y(*e ybvl/siThese 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 representsb uph:g bu w,ak- df/v43;mau0 the -R group in the molecule below? aub4dkm0ga-fhb/:p uw; 3uv ,

1.Draw a diagram of a generalw .b0r(,1y ofec*ohjn ised 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(bfe dw0y*f* d4q-9qaws) 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 influence the role t.vst21y4iwesp vzfys86 t)p; ij6p y; d7cl 8mhey play within the body. The diagram belop6 6; 7 2vzptscm sl 8j4.wytsde)v;1i8yipy fw 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.