Which of the following is involved in c-1wugy r x*na6arbon fixation during photosynthesis?

  Which of the following proteins is a hormd 1wx5 ecc 0 xb)gub;za18zhcym-)u0 oone?

  Biomolecules have diverse forms and struct82 dvlv;sg9s0;cgz) *ikzyb zures. Which of the following statements is faz; v2 )*ggsbcksv9 8z zl;0yidlse?

  Which of the following monomers can combine to form polypept8u (zp-pr;svk ides?

  The image shows a protein. Which level of protein s+b(jjp*nhg4 hhr2lc (n:jk 6xtructure is indicated by the letk+ cgnj4*:hj (l ( phxj2h6rbnter P?

  Which of the following is a distinguishing characteristic of tucv:5no5+l cb he quaternary structure of a protcu5 o:5vbl c+nein?

  Which level(s) of protein structure would be affected by denaturation due to h9w0k8tl 4hqtd igh te9kd4qh0 ttw8lmperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a9okiireu6/ ,w bv;v7v result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha heliakqv a-bkc(3 r.2b3alx and a beta-pleated sheet?ra3kkb.c-(aqva 2 3bl
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 t:rz7nm 2:vc ix) sfcv,he formation and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secon fuh r,k:e4e;lgp6wl5dary structure of a protein?

  What distinguishes the tertiary structure of a protein fr9ljjrlb4t48 ai5cc i6 y, v 48tmue)yjom the secondary structutml c 4it)jbaiy65c,j8jru y84 4lv9ere?

  What type of molecule is representem1 rf k(+b+t;fdaj s0kd in the diagram below?

The diagram below represents the structure of the protein ha,-um(a l c q9xgfx/j9+ ike*rfemoglobin.


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 formationfipl *r ;*:n,iver q1a of a dipeptide.

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 taken fr0p 43l- y;:ba9aqrzitphgvzbpi33 /pom the Malayan Krait (B. candidus) found in three localities; Malaysia, ;pa zi-0ib9p4gpha:rlv 3b3/ pyq3 t zIndonesia 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 crplgqgu, )hp /,0o z2as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then i 20ohr qpz,up,gcgl/)nvolved 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 grou335qn* xi 4-edgbrzi xp in the molecule belo5n*di-q i e3zgb43xr xw?

1.Draw a diagram of a generali2p:4yzt 54adowd zv s2sed amino acid, and label 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 correct for aminet,l sdib0sapr uvg2- /v93k4a m,ck0o 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 with 7r-v i (-s8ndyvltbp6fw(86uv+ (ckpwq1euqin the body. The diagram below shows an integral protein in the plasma memuie7 dpn- ( 6q1rs lvfuvwc kv(yb 86t+-(qp8wbrane 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.