Which of the followib 4i8moey6*w tng is involved in carbon fixation during photosynthesis?

  Which of the following 0uz uao/ .mj+nproteins is a hormone?

  Biomolecules have diversbjh ix(80 t3yse forms and structures. Which of the following statements is falsybj0sit8x (h 3e?

  Which of the following monomers can combine to form polypeptidegf e*nzb;n,3q s?

  The image shows a protein. W7 .r vbp8ep,ylh0+qcb inyu7c5:wky-ozx*, b hich level of protein structure is indicated by the letter 0 ,v5u :n.wbp-,xy kclizob7byc*r ehyqp +78P?

  Which of the following is a distinguishing char26tsua;r;8o hisatb 1 acteristic of the quaternary structura rbh;a sost;8iut6 21e of a protein?

  Which level(s) of protein structure wou/3o +vlablx8*; vtxgeld be affected by denaturation due to high temperaturebllvgx3 xo t;v/*e8+as?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of ak (zz xqbz8p j:jb.;h) dr+bj0 protein is a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between a(,mg;swy e sj5n alpha helix and a beta-pleated shees (wymj5seg,;t?
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 po jj+b fa,44lce8 soe*clymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following 99en py(p-f:qyfj5jo accounts for the secondary structure of a protein?

  What distinguishes the tertiary structure of a protein from the secondarrnqi9 eseo g52-1-zx; t fmkg-y structur qteg nz59;x2 -k-r -mgsie1ofe?

  What type of molecule is represented h +6m6(kxjsinin the diagram below?

The diagram below represents the structur pi,oten+n 4c6e of 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 di/ ;9els en3aig9jq.m xpeptide.

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 proteiq.p a03hm6qu3-9 x;5mn 07sm 7bvb scruawcrrn composition of venom samples taken from the Malayan Krait (B. candidus) found in three localitiesbnrq-w7 ma c9xq pac30r.br s0u3m v65mu;7 sh; 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 can be clash 9f,dd-lskjgf,3ghs4q /keq 9i0ja*sified as carbohydrates, lipids, and proteins. These molecules are of9/adq4ekgh,q-jh9sjsl *k 0dfgi 3f,ten 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 theu8s xrnjh90 y5 molecule belo5 9jy8 nhus0xrw?

1.Draw a diagram of a generalised amino acid, and label the fs b: qa*d70-deg o):guk.cg gtunctional 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 corr btia12lvii90nz:fx)4kl 4va1crbvx z1f-b3ect 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 the body. mi4z)s)g 4m)jly4ip cThe diagram below shows an integral protein ijg)4c4s )zlmim4p) yin 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.