Which of the following is involvedx ojgq3 32txqgp*;p 2h in carbon fixation during photosynthesis?

  Which of the following proteins is a veb ft7kdl+/2 hormone?

  Biomolecules have diverse forms and structures. Which of)d tecs :l5ay7l-h sjgt y88u+ the following statements is e8ss t-yla y8uthj7 +:cd5l )gfalse?

  Which of the following monomers can ce:99fv x8 j ptm1b8urpombine to form polypeptides?

  The image shows a protein. Which level of protein structure is ix);tzl, 8grr ody- dp7ndicated by the letter P?8p r-; dygdx,ol7tz)r

  Which of the following is a distinguishing characteristic of5u u;46u8d-yrz n.fj:aqqnkw the quaternary structure of a przu;- q.j:r 6dwa8y4 u kqnu5fnotein?

  Which level(s) of protein structure would be affected by denaturation due to hig9 q1f4qrgjv0;+wt cah h temperatures? f0 gjc+v1q h a9q4;rtw
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein iszu f3zbh.ol* 4/e gpc) a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish betweenxp n.rw7e5c1z an alpha helix and a beta-pleated sheet? xc e5wp.z1nr7
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 format k1h -;nz y3aid7ie8fzion and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure of a paid8pvt,c qt +( 8dwn8rotein?

  What distinguishes the tertiary structure of a protein from the secon)qd rl edo y3gl3pr712c*ygr6dary structure?3ylo*rqry)c7dlg 2rd 3 6gp1e

  What type of molecule is rep)1kfeu)00ai2ugngvu fz f/ +:dk a -ysresented in the diagram below?

The diagram below repree.glg86 nhyjvg8 p:2f sents the structure 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 dipep6+gs wf)00ygzbdom x,tide.

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 oybta9f ijp2b:j5zw 0 6c.o. yzf venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved at 2.ayb0.wz9i f jo6 pz5cyt:bjtemperatures 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 carbohydr76y)tretu 1dxsk 6hz5r5lz1n ates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different 66tx5 k11r) dlt 7shyz5zuenrmetabolic 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 bel5nejptz: g 2q)ow represents the -R group in the molecule bez2gtn qj5ep) :low?

1.Draw a diagram of a generalised amino acid, and label the functional gpj9/ebdn251k q fa , kvwn3vzt2a1lv;/)j x mwroups.

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 a1t) ko/hxknh5u8bve( mino 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 the2zzbeke2zo)0+kn 8b4:w f qx.t:ly ij role they play within the body. The diagram below shows an integral protein in the plasma membrane of a k0bb4k+y:2w j.8)o:tif2 l xzqzenez 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.