Which of the following is involved in carbon fixation during photosynthm17mk ot1 ug)ybscs :.esis?

  Which of the following protein +6v7f+okhr0 tcmmo1gs is a hormone?

  Biomolecules have diverse forms and stropdoo 2k; 3-9p sy;-/8qorl,yljesq euctures. Which of the following statements is false?e ,l;/2--erol;oyq9y3 odosqp k8p js

  Which of the following monomex:)jfc ui) t7rrs can combine to form polypeptides?

  The image shows a protein. Which level of protein structure is indicated by th3odw+ oh+dqrlt4c 10m e letter P?mw lco0h+d or4 d3t+q1

  Which of the following is a distinguishing characteristic hp bhcua724ct;8ns q7 of the quaternary structure of ab 284a7h; uc7n stcqph protein?

  Which level(s) of protein structure would be affected by denaturation due to hnf -v(-rr nz0righ temperaturn(rr0z n- rfv-es?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is :e2au-afl:,9 f jru udzo*eb)a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristickoxa0ob-: u o/:rw zr4s distinguish between an alpha helix and a beta-pleated sheet? bk:/rau4ozw0xo o-r :
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 icf6e5 3 4urgrthe formation and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the j14:seolgui i z3 zkz-nl6o95 secondary structure of a protein?

  What distinguishes th7 y6+ywt2sxyt xwlg,( e tertiary structure of a protein from the secondary structure y(6 7xstx2w +gywt,yl?

  What type of molecule is represented )3v;ytekief-wv/ hh ( in the diagram below?

The diagram below represents the structure of th,p0xd8g+wl ikolvt 0cd91w/yflvv4+ .jt8w ke 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 formatiobgb:* fg3(rcogbq 7a8 n 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 compositionz5/yl +g5 se5,nvhoo x of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transpor 5z,xhnogl esv y/+o55ted 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 carbohyddkum s1 o00- r:lh6hgfub0rw2rates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metabolic re0k 10ouds 0ubrh2m-wf l:h6gractions.
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 groupt 6qb9x v-skgx9 6nhcrn, wb)* in the molecule belowhns9,r tbn-6)gb6qk9x wx v *c?

1.Draw a diagram of a generalised amino acid, and label the functional gra; cnzgue -2*mn6o5da oups.

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 g; 2-dihs* kcqamino 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 thedwa+q-gwh f1pd8f (g, role they play within the body. The diagram below s q+a8wd(h1fg,-wg p fdhows 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.