Which of the following is involvedtxj;l+r) wk3d in carbon fixation during photosynthesis?

  Which of the following proteins is a hormone b (6bep.;f.: xbwn-jopvv)p k?

  Biomolecules have diverse forms and structures. Which of the following stat3 baqv 3gq6v6 ldsmc97ements iabdg 67clq svq9m3 36vs false?

  Which of the following monomers can combine to form polypewapy ywu99q 6c1 wf;z9ptides?

  The image shows a protein. Which level of proteine fs-kx jg :-6kmj1qf( structure is indicated by the lettxf1ks-(mjeg j:6fk q -er P?

  Which of the following is a distinguishing characteristic of the qua i6nz4v32oe7u vhe 0ikternary structuruev zi7 kh34v ieo20n6e of a protein?

  Which level(s) of protein structure wou9 a0zxv 3uu;elq ff lk19-p:cudb wb*5ld be affected by denaturation due to high 9e fp5zwdkcx1 ulu-v3bub ;0f9:l*qa temperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of whg-c9ud:nwga.xg i0sx1z8a5n ich of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha heli:j 2w,rraf yn3x and a beta-pleated sheetja,n r rwfy2:3?
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 and breaking zazuxz / /lg5pz0yq/i+ip/u0down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accoq4p , fcl8,r9;laekxpunts for the secondary structure of a protein?

  What distinguishes the tertiary structure of a pro*ai0 frwt;v0gj+ x*vqlf4 mayr2r,r1( 9 uzjbtein from the secondary structur0wfbr2lr az4r+yv gq;,*afjvxu 9(i*j 10 mrte?

  What type of molecule is represented in theh 6e (2xv.zeqq diagram below?

The diagram below represents the structure o/zsj;jh jw/ f9f 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 dipepti:bex :kcbpj:zciv-/h6; xn u(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 compo o4l9 jrromw*1sition of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported a 9*w1jmorlr4o nd 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 carbohydrates, lipids,lh(;/:gylxa a and proteins. These molecules are often broken down into simpler units y / a(;gh:lxlawhich 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 mo8et b ta zc+zyqxj ;fk/ )z;8mx1(lm3dlecule below? tz/ft aj 3)l8m;k;xm y1e 8bzq (+cxzd

1.Draw a diagram of a generalised amino d8ehxtt 93.z h8 a7hgy9.xhns 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) are correct for amino acid Rlqb*r6o 5t p4r-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 thynx qldg *m)6kznur b+f( o71;ey play within the body. The diagram below shows an integral protein in the plasma membran)6ymn +ognlkdx z7;bf(ru* 1qe 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.