Which of the following is involved i7rzj5 me x8i.kq, bb0h8m4aqyv 0k.x gn carbon fixation during photosynthesis?

  Which of the following proteins is a 02zeiinuz,* wn*1h2 az lwrj 9hormone?

  Biomolecules have diverse forms and structures. Which of thw;p60dkqdn7 k f8vu; rk65n-b yl5ihre following statement8 uf5 lq kryki ;b-;nk6n6rdw0h d5vp7s is false?

  Which of the following monomers can combine thbdf9-6l t bes-p. *sto form polypeptides?

  The image shows a protein. xr9*.,j chldqWhich level of protein structure is indicated by the letteqrj,x*ch 9dl.r P?

  Which of the followi++bt2 .gmf ymnz3 age+4 mrx6hng is a distinguishing characteristic of the quaternary structurfb6mre+gg + xh a+my2.tm34zne of a protein?

  Which level(s) of protein structure wouldwn4s.-ozw- 3vgye zqt n ij9,7f*jm; j be affected by denaturation due to high temperszt-*j9yf.jiqwvj4on; gz7 3e -wm , natures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein is ktbz u2tfvtiq0 )9.8la result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish bezz67iehn */yt tween an alpha helix and a beta-pleated sheet?eizh76 z/ ny*t
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 brea-u(;-v fbnqxd)n f m2yking down of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following a8zcv+,cb4mzy801h)ghx bvo zccounts for the secondary structure of a protein?

  What distinguishes the tertiary structure of a protein fr) )p8 pql8czy t7hwow(w7g wz-6xhko7om the secondary structure?o)8yw h7t)kw(lq w8-6zph cg7w o7zxp

  What type of molecule is represented in the dt.akz c6y-3vpiagram below?

The diagram below represents ti3dxpbvju;mt(,j )-kd (uf8h he 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 i9f0ait8/ 8g;;ihsux o* k celqe8zm 7of 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 tn wk+,wg4fo5 *p-tur ehe protein composition of venom samples taken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully transported and preserved at temperaug*,ep- ww4orn t+5 kftures 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 as carbo3lc9 +ipvo ic-hydrates, lipids, and proteins. These molecules are often broken down into simpler units which are then involved in different metabolic reacti-3 cicolv+p i9ons.
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 -r0 5zksrcar wt ya;;4x-2nge+R group in the molecule belz+agrn 5 s ;kxy-c0arrte24 w;ow?

1.Draw a diagram of a generayn-c5( zp 4ubulised 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 forg1r3hqv2ucv : v)*cgt 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 the body. The dieq,ci4nbt1ri h+ ,7u bagram below shows an integral proteiq u71nhe,ir c4ti,bb+ n 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.