Which of the following is involved in carbon fixation during photosv 1j d )3dauw)7n.yy7jgvf(a nynthesis?

  Which of the following proteins msl/6 cd,g i:his a hormone?

  Biomolecules have diverse forms and structures. Which of the follo0b+ f/9; e w,s4zljx ypv0qyetwing statements is false?0yezq l/s0 + xt,y4pw fj;9evb

  Which of the following monomers can combine to form polypeptide;ryk c-abf;i -s?

  The image shows a prot)mlt4ft 6g3t vj)wdrnc7 nk9bvhz *35ein. Which level of protein structure is indicated by the lettev6j4mn z7rwhbd fkct)9 5tv* 3tg3)nlr P?

  Which of the following is a disi0 s :.qpcln0wq-ol*btinguishing characteristic of the quaternary structure ofl 0psqoq:0 wlc.*ibn- a protein?

  Which level(s) of protein structure wo0+ v;gy *)wjjyhyi r r.oh6e1luld be affected by denaturation due to high te .0rljyoihv y+ej1;)wgry* h 6mperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of which of the following: 5t/ y*) rn jnkixm35ll7aal4k
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics gze,1b9h1q cj distinguish between an alpha helix and a beta-pleated sheet? , g1h1ec jbqz9
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 sy+*yx4 nhau dlue.btr z2/15a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary7 u ,oakfqnfa9ic )h1( structure of a protein?

  What distinguishes the tertiary structure of at9: lh b2pm/l qe8fvl, protein from the secondary structuhv b9fm /tql8: 2plel,re?

  What type of molecule is represented in the dv;-gn, rdr d7gfbq. *iot3r,x9pwqb+iagram below?

The diagram below represents the structure of 5wfuvnl2;+*- pv lwzmthe 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 dipeptide.;zt.p: (tmxk:ncmq0 x

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 fp1uz2 u hra.usd5)6quf2 z1gqyhn/8 protein composition of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysiahu6hzq1fyua 2s281gu upz5fd ./q) rn, 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 classified as cs5u+x z6t 4z-s+sfgdv arbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metas +6vt s-4fuzdsg5z+xbolic 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 in6e 0kwfv9rig q14svy1 the molecule bewg4vr0k e1v96fis 1yq low?

1.Draw a diagram of a generalised amino acid, and lab ms 1yp ha2-7w:abaq.gel 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 sta1,a1:c tiw clftement(s) are correct 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. Th9yi6ite/ c voa,ajroh)( sk9,e diagram below shows an integral9iv9ki,raja t(6 so oy)/ch, e 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.