Which of the following is involved in carbon fixalav :+ho 5d6artion during photosynthesis?

  Which of the following protei( wr9;/q2j hpkmru2x uns is a hormone?

  Biomolecules have diverse forms and structures. Which of gpo0:otkuhli2+ c sjun8a, jgx, 98 s0the following statements is falspunlj+ ,kg8:u hj0x0a , ts8 so9cog2ie?

  Which of the followic , wu6-jj h.xj4tq3njng monomers can combine to form polypeptides?

  The image shows a protein. Which level of protein structure is indicated by thegki e4jg9 b5sk) *jaufsd4bt3 8-l3ir lb *)u4sisb34jjgtk 5 aekdg r83f-l9ietter P?

  Which of the following is a distinguishing characteristic of the quaternb3 jsy7buv.x8y/q 0zkvq /an; ary structure nj0.8/xz;a vv3y q7ubskyqb/ of a protein?

  Which level(s) of protein strucm*w hosdjiv,53 ma 7+wture would be affected by denaturation due to high temperatmdos7jm3 5,hw+ vi*awures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is ;kb*:s o)bazr) yjt5 ta result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an a9 pi+u6dsa wn7lpha helix and a beta-pleated sheet? 6 p naud7wi+9s
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 p+z,m m:le/vt the formation and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts9fzih*dl 1;,fw j4tux for the secondary structure of a protein?

  What distinguishes the tertiary structure of a protein from the secondary -kg; t7bn6tv/fl(m1p +;rkg n/ ayouastructure? n7t/ bl nko;g/y+ptfuaavgkr1 -;m(6

  What type of molecule is repr y)si cv2k5gfh8 duh9,esented in the diagram below?

The diagram below represents the structure of the proegg80m7louf 7ejo wj) xw:s 8f:6rtsh;1cou :tein 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 diq* 8(8esi 00mx pkex-0xgkx zupeptide.

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 compo lghvxs 5s4+pb4g.)hlsition of venom samples taken from the Malayan Krait (B. canh l .sv) slg+x45phbg4didus) found in three 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 metabolism cavs;5 p e z*uv-fjzg; x1plhy,a:ea:a(n be classified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in diffz a(;l:p5e v*juph1fe;svx:, zyga- aerent 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 moleculy40 npcszgq92qu+ -bv e below?psgb2q40vz 9qu +y n-c

1.Draw a diagram of u lzzky5:7a3ja 0 17.knauufp a generalised 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(s) qj/ -ihrs qe88are 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 they play within 796c+f* qgknx r4+odr vqg.tq the body. The diagram below shows an integral protein in the plasma membrane of4 noqg.dr xf+ 9rq7cgt6k+qv* 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.