Which of the following is involved in carbon f6k (lyqf d6fr2,l6j biixation during photosynthesis?

  Which of the following proteins is o;30 dzp4dzsv i2vb -qru,f; smd0o7ca hormone?

  Biomolecules have diverse forms and structures. Which obc2xwha-cgk, *s3dx7kl9 x5 k f the following statements isg 93l c5 xc7-kaks kd2h,wxxb* false?

  Which of the following monomers can combine to form poe se;ysaapq-r :937gwlypeptides?

  The image shows a protein. Which level of protein structure is indicated0wst+sh2a +9j sf3m 7lbw tc t/y; g1ln94krgt by the letter P?bcf9tn3mg71 wwtt r h94sy/+ak;sl+ s2jtl g0

  Which of the following0 0biy7 s a5tus7-xlym is a distinguishing characteristic of the quaternary structure of a prsb-m xy0 ly7usa7 i05totein?

  Which level(s) of protein structure would be affected by denaturation due to xe35l(zvvd6s iq;ni6 high temsx;d(v 6n35 6vilzqie peratures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structuram vnmbst*/,w f(s: n.e of a protein is a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alphb4 dev(eafm 4:/j*: *pyb 9vabzgz qt;a helix and a beta-pleated sheet? ( f:9meybj t*:vzqava/bp4 z4g;e d* b
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 breakiwz gortr4a jg.* /as2w-.dx x0ng down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary strpr4aeyc-m;q +ucture of a protein?

  What distinguishes the tertiary structure of a puq-5t -5q jotxe)kc(arotein from the secondary structuret-q)ex5(uq c a o5ktj-?

  What type of moleculeiv-: hov 3yx2z is represented in the diagram below?

The diagram below represents the structure of the protein haemogx6(fe9e yhv6 5fs9 b 8tsjkye6lobin.


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 u 27zwrdbl4 v3of 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 8q (hnht)gup* n:1g86u a zzlrtaken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All sampl uau )q 8g8hnp(tgr*zl61zhn:es 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 at0zlcw+ nldfh 5.9 d rbz,26hms carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in ditll 5r.zz690mbc +2hhdd, nwf fferent 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 0x,i:8 xb y9ca3fxx yithe -R group in the molecule baxbcxii083xy 9x , y:felow?

1.Draw a diagram of a generalised amino acid, and label thezwf +aj 2jk-b48fj5 no 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 amino acid R-groups? 9p5h02 aou i4eefklr,
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 td08bo)8 ftd)jil l l9cr9wajuf4/. si hey play within the body. The diagr u/f8it ld drwc08bj.lf)s9i9j)a 4lo am below 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.