Which of the followings ias.eq su(77 is involved in carbon fixation during photosynthesis?

  Which of the following proteinwumns :op3x2 m2ltt57s is a hormone?

  Biomolecules have diverse forms and structures.i;52y 7h xmz:3vmxabg Which of the following statements is;v: h3m7xz b52axm iyg false?

  Which of the following monomers can combine to form polypep*afypx s2u,j gd -9(n,gnsz1ptides?

  The image shows a protein. Which level of protein structure is indicated by h z)tbjenenzq7--xv5lk p xg0(7r92cthe letter -rvlzg 5ezk pjcx7b-7et9)0hx q 2(n nP?

  Which of the following is a distinguishing characteristic of the quaternary soq jr5gz9r t:c;x/ -1kl sixkr)d6sd0tructure of r r-1xgzdqr/5jcloi0xtkkd 9s 6)s: ;a protein?

  Which level(s) of protein structure would bhqt)q0h, righgnrqup 22z8: h0o0 hs1 e affected by denaturation due to higq8h, gp h20rng s:z 0q2oh0qiht rh)1uh temperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result m:b-atpgk+ v9zvw7 t4of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix i-e1kc;1h,p/jpy)k kw / nrghand a beta-pleated sheet?// ikh ny,1-jh)crppk;e1gw k
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 breakingmx: : necirv00whfj /. down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure qql:ddi)g*g ; of a protein?

  What distinguishes the mnw*+lcr84 7uycq5wttertiary structure of a protein from the secondary structurc78 *c5 umn4q r+wltwye?

  What type of molecule is represented in the diagram ):n hop 8;a.mpu) exvuyi0k*abelow?

The diagram below represents the structurn6 ,mcaw3 e 3hzggm1ix( h,1gae 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 dipeptidj b5mt.jvs8e ;e.

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 jhv /r- fl4 -2qeekb+ztaken from the Malayan Krait (B. candidus) found in three localities; Malaysie/ 4zj-vkebrh 2f-lq+ a, 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 be6tisjr ++b s*h classified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metab +s bjst+*6hirolic 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 followi 5buj(ua 5pju8ng structures below represents the -R group in the molecule belou 5uub5jpaj(8 w?

1.Draw a diagram of a generalised amino acid, and label the functional groupiliqw+ ovb-c9j/ l; e)s.

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-grou;:z pge njjb6k); ct8ixv/q6 hps?
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 thefjv( d:7c574dhe czr z role they play within the body. The diagram below shows an integral protein in thejdc75 rz cd:4z( ehfv7 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.