Which of the following is involved in mfx8f,w/c 2k+gaopm*x m:ib.cxm/ 7s carbon fixation during photosynthesis?

  Which of the following proteins is a*hqk j,vizs(urp()/q g5bcs+ hormone?

  Biomolecules have diverse forms and structures. Which of tfzp5 jax2mzs9084 j bjjb 6 .2zjvhv)ihe following statements is f562)j9b vj p8vxz shmzjz0 ij2. b4jafalse?

  Which of the following z y gg0k6aboj9(nh46lmonomers can combine to form polypeptides?

  The image shows a protein. Which level of protein structure is indicated by the 4ge mmxsf5jx sm)2 0/dletter P? 2/es4x 50gxfsj m)mmd

  Which of the following is a distinguishin d 0q5djv en pf*kd0ka5x+1md6g characteristic of the quaternary structure of a m q1kkpn dd*0 e5vaf+0jxd5d6protein?

  Which level(s) of protein structure would be affect73o298jt8 jcwf0s hvc7kll m-v e+ hiued by denaturation due to high temperath 9t ek3v0+llj m7huf 8i8w- s2oj7ccvures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of which of the fol+0zy m:r) z.*hoq nveelowing:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix and a bze/ bmalqysglqn*3 ;,ac 5( *re0b 4pveta-pleated sheet b*ga5mas3e( 0ql c,qrpz;*l/ 4nveyb?
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 down of a pol hrj5c1 (lyxc.ymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following acco+ bee.v:m* b(zc3:x -. lfrtfmsyk hq2unts for the secondary structure of a protein?

  What distinguishes they mldqv8,* a7r +9fqnm tertiary structure of a protein from the secondary struct+n,98l *q ma vmrqfyd7ure?

  What type of molecule is represented in the diagram below? jbh n)ucia-mu:ajlt 0vaeg 53 y:86:b

The diagram below represents the structure of the protein hae 2hxqp1otj4y:h u .b5qmoglobin.


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 dipept4nz qwtb7+2d esx6,foide.

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 taken z2v7z(1w6 rm vc(pessv3m4zp from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carezsmv pc7mrwe16zp 4v((vs3z2fully 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 can be classwr vwvo a. pm5v.*7j+x odo(u0ified as carbohydrates, lipids, and proteins. These (voxo5pw0jrv*7.u o a .d+wmvmolecules 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 represents the -R group in the molecule .yf 8m xiil7;i5nzo yh6y*8-g chuw4lfzb4;vbezzwmi *-vfyh68ib;7 4ll4g 5;ci h . oyf8nxuylow?

1.Draw a diagram of a gener7mre bt9dlh7oq,n+ owl ogeb4d,t :8. alised 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) are correct for amino acid R-qo m*1zk6ls/byb 2d1v 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 the body. The diaaizh8e /a- ss p/4hkv 4tyq,6zgram below shows an integral protein in th84/s-t sv a/z ykei, phh4zqa6e 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.