Which of the following is involved in carbon fixation during yedv.:6 (i8 esg- hzm8u1ti elvci; f5photosynthesis?

  Which of the following proteins is a hormk4o+b zjs2tv t./ye +wone?

  Biomolecules have diverse forms and structures. Which of the following steqlbtz,o11rzu / d8lu12hi ,n atements is ,otunzrh2ub1/ iq 81dze1 ,llfalse?

  Which of the following monomers can cylf+ 4nf xb18./rxlh 49jao lk)t of)combine to form polypeptides?

  The image shows a protein. Which level of protein syh ye7gtgb 6:gm;(2bjtructure is indicated by the letter P(ymjh:eg ty6gg2b7b ;?

  Which of the following is a distinguishing,:k g1rpvhv 0e characteristic of the quaternary structure of 1e ,rg0phvk v:a protein?

  Which level(s) of protein structure would be affected by denaturyrv/ hsw4.dy.fk s( q)v8mda6ation due to high tempera vh()m.qsys6/kafd4dr y. 8wvtures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is av *qwrnv3.yq:nm uydn5o+m1; result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix and a beta 9wap co71o3lgut1yue82z4o.kjc7 p o-pleated sheeo7 leu8p 93a1poozg12 4.ckuctoy j7wt?
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 a poly2 f:lz npa 0;q o6it2axd4j;wfmer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary s)c;2 yme2 4 tc4brmitstructure of a protein?

  What distinguishes the tertiary structure of a protein from the secondaw:i 9*7 hp rd3y1gipn4lih ud3ry structure?1pdipw:7r3l hi dn*h3i9y 4gu

  What type of molecule is represented in the dxi b* lzmrl2i)d-o+g)rq 8wv;iagram below?

The diagram below represents the sta) favy - u bbl-2-(r/gicf:owructure 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 dipeptid:xxk3:iq 9lg i onjr;4 *f bnh4-qre+ve.

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 ,v* ajbyf i6u(m-h+x0dcbt: r the protein composition of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transportb*u, riv+x ac(fhdb6 y:-mj0ted 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 classxr,/t 7u5z ifeo- hds(ce h5r1ified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units7sc/zrh-5 i1f5o ,etxhd( ru e which are then involved 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 t3cypu8d l+ 5 wh1ms,oshe -R group in the molecule be+du3m8 1wol5 c s,spyhlow?

1.Draw a diagram of a generalised amino acid, and label the functb: i;ul 4p 6b.vx6gjnwubp.w4ional 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 statementnyg:r cqcn,-1 u/uin9 (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 thku8y4if w0tqim:sj7z mx8+e*(nw 0a te role they play within the body. The diagram b80wx f nu+sw470*t8m(:miz kejiyqa telow shows an integral 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.