Which of the following is involved in carbon fixation during photosynthesi f4k/ wir,k3grs?

  Which of the following proteins x/ q7 (;rqw3kn8sdy +fc4y exlis a hormone?

  Biomolecules have diverse forip lybdb5 ,9le/ gu7b8ms and structures. Which of the following statements is f,eilgp/bludy98bb 75 alse?

  Which of the followinglaccya2bo z07c58jrnqf9g9t+x + x8g monomers can combine to form polypeptides?

  The image shows a protein1zkgyh,;cbcqbu,x0 2 amcjd14 4 ry9 d. Which level of protein structure is indicated by the letter P? amhb gjb10xyr4 4;k9,,u dzc qcd1y2c

  Which of the following is a distinguishing characteristic of the quatmrpo4l( s f0y:ernary structure0fps :lo4y(mr of a protein?

  Which level(s) of protein structure would be affected b-pcm( u;v j1ag17mviw y denaturation due to high tempev(a m71iwpmcj gu;-v 1ratures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result oig5z74)8 bvg8kjw/jgdwr 9u. +d gktsf which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distingunw byg7f7 qb+-k ti00wish between an alpha helix and a beta-pleated shee00b7wk gq-bwyft +7int?
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 form., cc rulfnd lc,y*-6:iy4o jwation and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the seco,c h,tev45ajz h w4*zindary structure of a protein?

  What distinguishes the tertiary structure of a protein from the secondary w(fl*hmm) .yoet ( u*2u 4eho *:egvokstructur*ow)e fhv.go yk uum(*(elmo t*42h: ee?

  What type of molecule is represented in the di/a7 uuwb6 qaf*agram below?

The diagram below represents the structure of the protein haemoglobgj 1l,m8; 8;k+lai2lan jgkarin.


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 dix 4w 11n.8nbpxl- rltypeptide.

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 comvy9(vzm3l3 j dposition of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia an mjz9ld3v (3yvd 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 carbtm6dmqwv)d3 ;jl el+2ohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different meta3m6 ;t e2q dv)dlwm+ljbolic 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 struc3qok k3,jf m2ptures below represents the -R group in the molecule belo3 qfk 32kpmj,ow?

1.Draw a diagram of a generalised amino acid, and labeec :zvkyoq+oeu1t* uqx-8 1tr9/g r c:l 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 statement(s) are cp:ep 8o)adazvp) uw2f9,cy4eh5 tl a8orrect 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 wes*uh 7. gjar9ithin the body. The diagram below shows an integral protein in the plasma membrane of ar.9se* ahgu j7 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.