Which of the following is involved in carbon fixation during photosy49) 5r t1u6:w k0jao. )ldlkhjgqcp cjnthesis?

  Which of the followinnv5e+k8hk k8f g proteins is a hormone?

  Biomolecules have diverse forms and structures. Which of the following s(x1 0ay.jbr ywtatements0b.ajxyr y(1w is false?

  Which of the following monc+d7mliwlk 8/ omers can combine to form polypeptides?

  The image shows a protein. Which level of protein structure is ino8520q7 vc )iuswrklh dicated by the letterquwv0r8k5lh i)c2s 7o P?

  Which of the following is a distinguishing characteristic of the quatela oo4vub 9q, 9n81c14s wga f+z)mifqrnary struos1z g)8a9 iqc 1mqv lfbw4+9n4uof ,acture of a protein?

  Which level(s) of protw7x ho:q+q mpv1k t j /;v0w0pmvx tgt9(93rpeein structure would be affected by denaturation due to high temperatures0v:xo9p 7(q g+ k0mjt pw1hvpm/xt3r;ew9tqv ?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result oyjde4;aw( z ;ef which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between a 1 v02r2etm+:dfcya znr3vvl 6n alpha helix and a beta-pleated sheet? 0vr 3dmlaz1tr6v:nc+y 2ef2v
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 downxi 5l5q/9g)1oroi8xbh:y kdo of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts3i pwrtq6, f d)a*rt+.2 /qtelpn, cmb for the secondary structure of a protein?

  What distinguishes the tertiary structure of a protein frxx )hvmob -97rom the secondary structux9 7v)ohr-bm xre?

  What type of molecule is represented in the di3lys cb yg;w*ztz// (oagram below?

The diagram below represents the structure of the protein 6u39f4gya xr*dw fj8t 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:dpykwn (sey-p8+:* tc vvcf) 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 fqbvtgh/d:4n ig 0h *h7rom the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved n7/hgq:idht *h0vg4bat 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 clasrt;(pnj+/ :0 gqxvqxfsified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in diffrq ;v/ j(+g0 x:nfptqxerent 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 group in the molecule izh :wf bu8z u6/:f7oob:/o8iohu fwz u7f6z :below?

1.Draw a diagram of a generalised 6ex,vq, a kso.ju+9 uosc 2+vph3tc:v 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 statezp d htc1eeqy3djv+c355-d5z4 sfou3 ment(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 thgw3dj33g1wiv3n 11v61e;h gkwk xru g e body. The diagram below shows an integral protein in the plasma membra;6g3x3 iw1rug dwgke j31wg131nv kvhne 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.