Which of the following is involved in carbon fixation during photosynthesc-b dr,4 kxj7f3ggkm.is?

  Which of the followingj0rtrq, 8ndnv9 4fj/ q proteins is a hormone?

  Biomolecules have diverse forms and structures. Which of the following statemp ;5 3lw/9kq 3tqof1tjwzkea*r)xi:f entqj3:k)19aw;kql t /pf5*x3frt io zews is false?

  Which of the followi/0xr5 f e8).ixzwat nbng monomers can combine to form polypeptides?

  The image shows a protein. Wsg5 (,6ke 9/ kmfgylmon-u9qdhich level of protein structure is indicated by the letter yu/de nfm6m ko,ql9 95( sg-kgP?

  Which of the following is a distinguishing characterisfaqh)ykw u nob lj0s4m:.m/qqk,56+ ytic of the quaternary structure of a prokj:y yq6 s qbulonw ,a5mq)k4f0/h+. mtein?

  Which level(s) of protein structure would be affected by denato9;wb.n 3 orv jc/iq(oxl:*dwuration due to high temo x:*/( wji9qo c;dw3.v onlrbperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a pro (er;i3+pftp:0gmgq itein is a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish betweesr5 ar5jo ,yq/n an alpha helix and a beta-pleated sheet? 5 j5 yqros/a,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 the formation and breaking down 8vca pj5/;txj - ib:qnof a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary st afo)ur- 8dh3oructure of a protein?

  What distinguishes the tertiary stru kud p0r8y8s opwl(dm(93z5fmcture of a protein from the secondary structure?d5zusm88m p0(ol 9 wf3ykdr(p

  What type of molecule is represented in the dia/q ccfylgc6d/- (h .c9io8xyjbr 1j, zgram below?

The diagram below represents the structure of the protein3weeo tz) 4*yj 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 format8qsrk*i3h8l b4d sl0bion 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 composition of venom samples taken from xa* b*g:jw,hjig*qzo0 l /c*w the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved at temperatures bw*hj,0qi c w*x/j*g agb lz:*oelow 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, lipids3 s( 9c-eqhlqd, and proteins. These molecules are often broken down inthqdec9sql (- 3o 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 represeoke h cqk33*)ynts the -R group in the molecule ok )* yq3ke3chbelow?

1.Draw a diagram of a generalised amino acid, and label the func r9;m8ypn4ith km r t8frj+)(mtional 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 aminomzhb* s)e0*w j;*: dr6ijq qwvhac6,g 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 withihb2klb;/zqf kh+1za8 4r si2g n the body. The diagram belogkarbk2 2iq ;f+s 1z h/8bhl4zw shows 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.