Which of the following is involved in carbon fixation during ,5*rn ogwf:o hphotosynthesis?

  Which of the following proteins is a hort n7:sh f4b4uu69 dzqxmone?

  Biomolecules have diverse forms and structures. Which of7)2w2vfiuc mdl0riks9++cr q the following statements is falr+f+id ukc vl27 csrm90 q2i)wse?

  Which of the following monomers can combine to form pu u0efgjap:8,olypeptides?

  The image shows a protein. Which level of protein s ids8n-g nk4 l.6kkwkuqd6f obyst 90/1 *et8xtructure is indicated by the lxuo ygt. 1*klit bsds68 n0qw/8946k dkfken-etter P?

  Which of the following i-rk dy9 z3d-dy/kt-s*4fxwzv7wb :its a distinguishing characteristic of the quaternary structuwv47dz d*x-ikfr / k-t-3b :9ywdstzyre of a protein?

  Which level(s) of protein structure would be affected by denaturaxl7x o,ub9av2/u;v4 s8 axkcs tion due to high tes2uus vvxl,abk;/x9 ax o7c8 4mperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is a result of which of the following: js3r0 fps6pr(
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics disth+tmie7 9oz l)inguish between an alpha helix and a beta-pleated sheet?)lt h ei7m9z+o
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 (n8icokilmqxm1z9b8k z 4*k )and breaking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondaryhx*xle+/q *lx,/z4rz e m(s hz structure of a protein?

  What distinguishes the tertiary structure of a protein from the secondary p.nm;sh+g13 w/ p30ruib6 oruzrve (jstruct+0 hjg morvwe(p/1usirznu 6;. bp33rure?

  What type of molecule is repres gfzmq gy4;ak;9x2r (aented in the diagram below?

The diagram below represents the strucetw6nnfs7+(gxzz;uj . wv2d3 ture 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 dipep3-tv +rfffda+ tide.

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 compositiondo0:;m 9ta ) pdg+zcog of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indon+9aogz0m;ot )cd:pd g esia 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 wt,:dvhyz(*qz+pg,vclassified as carbohydrates, lipids, and proteins. These molecules are often broken down into sipqd :gw zt(, ,h*yvv+zmpler units 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 the -R group in the mole n9/mjp cu *-ksc(lf,hcule below?kc*c h9pjfnlsm- /, (u

1.Draw a diagram of a generalisee:0 aajjwhrm *y.8 n/ fips w/;et6xn:d 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 cor0y5 zalgybkn z 40uc52rect 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 withiwbt5s6htu1 o v* ls82mn the body. The diagram below shows an integral protein inhtvwos u26sl b8 mt1*5 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.