Which of the following9 thf,zen7zp- ,4zlel95y vn g is involved in carbon fixation during photosynthesis?

  Which of the following proteins i 3z1r4;aqg jxks a hormone?

  Biomolecules have diverse forms and structury 8qqc28jg6l(9u,9mb bqp.fey+ad dhes. Which of the following statements i6+qe 29(y9qg8,djbau cb l 8y.qphdfms false?

  Which of the following mono zcs;xt,6 snz1mers can combine to form polypeptides?

  The image shows a protein. Which level of prothz9ksw1,aeons9upao (9 * (sg dta((zjx2fk7ein structure is indicated by the let so2( wgn(91a7z s h*tfd,oepza99k (s(axjkuter P?

  Which of the following is a distinguishing characte/ 6s xvz jya(l:/py-dgristic of the quaternary structure of a/l ad xs(j6v gp:-yzy/ protein?

  Which level(s) of protein structure would be affect ;p0 jpq86yppved by denaturation due to high temperatures?;pjv6q ppp0y8
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structur14o7 pfywc*wx l1m u9ye of a protein is a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguishitahdde09 ldpu kiy:8/15 gu* between an alpha helix and a beta-pleated shee kigd08h5ld*d9:e u1/a ytpuit?
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 doww :8xys47jvxl8aeu v4n of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure of a protein?gb8m:z 0ca,+uvrnqf9

  What distinguishes the tertiary structure of a procvi r qx26(tn.h ehs29tein from the secondary structu6hnxqv 9rcs(het .2 2ire?

  What type of molecule is represented in the diagran57 7t5 rdmoqnm below?

The diagram below repp(.z,0 lv4i;jnjqffqresents the structure 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 k2( g8intejkg;x, 5mu 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 jlc.phg*zc *ucy(7c : )uf(dmprotein composition of venom samples taken from the Ma7)p(g:d.c y*cu c(mzjuc lfh*layan Krait (B. candidus) found in three localities; Malaysia, 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 metabolism can be classiktxk heqt(c84r,anprw:aav0 apqw( c a2, 642fied as carbohydrates, lipids, and proteins. These molecules are often broken down into simpler units which are p,h 2kwrpaqxct,tanaer( a08v(aq 4 c:2kw 64then 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 the -R group in the molecule w-iwkdno 5hjw+-7 9 lubelow?nl97+5uw - ij-odw khw

1.Draw a diagram of a generalise;rai-;m o:q8 j).g jf se(oyejd 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 amino acid R-gr; z9uch:g8/avy2wf dx oups?
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 proteinsy6)hwg )l1 oqk influence the role they play within the body. The diagram below shows an integral protein in the plasma membrane of a celqw lky1 ))hog6l.


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.