Which of the following3tzl09w:c6oewtbi +g is involved in carbon fixation during photosynthesis?

  Which of the following prote. azaw. f.dp7vins is a hormone?

  Biomolecules have diverse forms and structures. Which of the follo9z/n0i f nfeuhuavv i83st/8- ipv+k6wing statements is/z8 i3vhut06ina sp v-u 9/n k+8efvif false?

  Which of the following monomers can combin+ ;qopf61mn dwmz2au*re5+jxe to form polypeptides?

  The image shows a protein. Which level o1uk /6ch/a2/ +sc bfv;xksww dh+f y0jf protein structure is indicated by the letter P? f/h/fbw+0cs6 +u/xwyak2kvh1jsd ; c

  Which of the following is a distinguishing characterist45b;e i28mtod0ief gg l/jj9 hic of the quaternary structure of a proteine;t0 jgh9i ojle842b i/5g dfm?

  Which level(s) of protein structure would be affected by denp)pz 8lbh:o(nfz m*8taturation due to high temperaturm bo)p*nz88l ( tzfhp:es?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of ts, ud7pe:tf0nej hpe5 -5)kx which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix a luxb; p7l 8ctu4hy,.jnd a beta-pleated sheet? py,uj4 8c.xl bthul;7
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 teo .iaf q0.aii-46gv 2v1,(fvkhie c dhe formation and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accoy ,s t1f/thes*unts for the secondary structure of a protein?

  What distinguishes the tertiary structure of a protein from the s;5ue9s:hn eg 1j yug1mecondary structujg 9ueuhgn5e1s :m1 ;yre?

  What type of molecule is represented in the diagram bel fe 8vr6ja2xie5b(w8r ow?

The diagram below represents the stru m-laywfka5+,vvrr v 4r,mw-1cture 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 at d okaww)x1um1/iq5 zy)6 2hj 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 venom samples ta64x.r t* ,aejq6hkycgtx 6lc- ken from the Malayan Krait (B. candidus) found in thrq,gl x- jt 4a6ex6 .ry6ck*htcee localities; 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 metaboly5h mm d-u7cp4ism can be classified as carbohydrates, lipids, and proteins. These molecules are often b4yu-5 m7c hpmdroken 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 represents the -R group in the vvd 9znr8n6 w- nwp(8hc*ok)bmolecule below w9n (wko8d bvv)z-c*n6phr8n?

1.Draw a diagram of a generalised ami 2ekj e*e3*sok dtfle/;fq/j kg,9,kn5a9bsh no 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(s) anj zsuw 7 )0,:rrrab/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 infl6jz dz4aqmb)d h0;m o:uence the role they play within the body. The diagram below shows an integral proa;z 0b4 ): qhd6zjmdmotein 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.