Which of the following is involved in cacf-82n nq7h7 zf idod8rbon fixation during photosynthesis?

  Which of the followinv ptu8kxuz- x-)lt *5:yhkor. g proteins is a hormone?

  Biomolecules have diverse forms and structures. Which of the followinjx(4s p(q g)kx df.yz1g statements is fx4p)fg((.qs1dk yx zj alse?

  Which of the following monsax61pcc: 36yc1 heeypf d.p1omers can combine to form polypeptides?

  The image shows a protein. Which level of protein structurogl, t64-d gbi 7cv2aae is indicated by the letterv2lt-i ga4gd7o,6 bac P?

  Which of the following is accm4uxq3/ y4pm2m**bz eo c5g distinguishing characteristic of the quaternary structu3ub4 4c /zocegm*x*qm5 y c2mpre of a protein?

  Which level(s) of protein structure would be affected- vmuh7vrvk7(r1fem+5nl w :i by denaturation due to high temperatur5u1n e(vi+mw:frv- rl7m h7 vkes?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a re gkh m xyf,0j;iv(ep:/sult of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish betwe + i7(tmjp/l07* tyn3ew uhlg sm+ngn4en an alpha helix and a beta-pleated sheet?tl p7+ gs30yulgmi7en(* jn+ nw4th/ m
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 ay2 epa+v9 flqi:0h1ut nd breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure of p5gsa csx*3 w-a protein?

  What distinguishes the terti-o3h agp -6lw0yasp dw9eap5pnk1m 5)ary structure of a protein from the secondary structa p9y 5egppd5w0ka)61p n- oms a-h3lwure?

  What type of molecule is represented in thu,twqg.d03s op l :4,dz4km/v5 rh2h6qap lnne diagram below?

The diagram below represents the structure of the protei8:ha y+f5gw+bx ;y;lv5z mj ein 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 formatz )rce6bxm2k -1qbk8 lion 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 fro3wdfsf mc64 z6 uao99..lhsptm the Malayan Krait (B. candidus) found in three localities; fh3z l4a mtc..s6du9s96 fpowMalaysia, Indonesia 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 metab4p /rdby8w 6rxrvl3-c 0 rho-eolism can be classified as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metab v8wrh- rxr0yp blo34c 6-rd/eolic 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 hgv5/dpn v4 5 re:93./rhb wjr rh1roathe molecule be rrp5 .4ne 3gh 9wbd1rovhr//j:h va5rlow?

1.Draw a diagram of a generalised amino i(n:ag:) .aq c(ejsc 3vjd r2ptbhk;8a4 af2kacid, 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 c3dski4r0*j k b*/dnzo/ kctqmosf0--e v/r/ u orrect 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 i(t-u qq 4itlq2/ccr1b;a +taxnfluence the role they play within the body. The dia-a(i4c tbqcq2 qtr;u xt1 l/+agram 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.