Which of the following is in 9d629f-df d,pmbs:bi2c oocz hfu(,d volved in carbon fixation during photosynthesis?

  Which of the following proteincis-+m ha(hdcf9j x t6j.1lt)s is a hormone?

  Biomolecules have diverse forms and strjbmal j4d3 h;l7w b5*) sjpo:fuctures. Which of the following statements is falj *j4ah:5df) wp ombb37s;jllse?

  Which of the following monomers can combine to form polypeptides? -x3xrktft051 x az3zt

  The image shows a protein. Which level of protein structure is ind zj;4tsc ejz: xe;4-ihicated by the letter P?j;ht xzs 4cj;ei4- :ez

  Which of the following is a distinguishing cha+ d/x 2b h90n48q:umvnix mejtzkj p v)h(-x4hracteristic of the quaternary structj:4m u82-9 h/ij ezkdmx)n+ pvx (vnq4xbhht0ure of a protein?

  Which level(s) of protein structure would be affected by denatura7, 3bvj;adgyud8 e7jzk tt:4t tion due to high t k az8g3;utej 7d4tvjb:7,y dtemperatures?
I.
Primary
II.
Secondary
III.
Tertiary

  The secondary structure of a protein i sca1pwt; 7 de:pys(k0s a result of which of the following:
I.
Hydrogen bonding
II.
Covalent bonding
III.
Ionic bonding

  Which characteristics distinguish between an alpha helix x tszk(/j5y )nand a beta-pleated sheet?znsx j y(/k)t5
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 d ) iq be6dxw7aj,a0q7v*km/l3ds( ice0mr pq (own of a polymer.

2.Compare and contrast carbohydrates, lipids and proteins.

  Which of the following accounts for the secondary structure t y,ac4g5oa;iows6zj .u46 jeof a protein?

  What distinguishes the tertiary structure of a protein from the second;1- o 9bku8weyfbsa +vary structure?y;8o eb+sau9w b f1kv-

  What type of molecule is represented in the diagraz.c;w+w -*mk7zzoqo xm below?

The diagram below represents the st6 sbw5hkr 6/dgructure 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 formatyn7;72du:e kzd moy+ sion 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 t6zqq/pv3zf,yd3vn( r aken from the Malayan Krait (B. candidus) found in three localities; Malaysia, Indonesia and Thailand. All samples were carefully trans /zp3zvd3nqf q,y6v(r ported 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 classified as carlw/3.otsox; hbohydrates, lipids, and proteins. These molecules are o;/lsh3 twoo. xften broken down into simpler 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 bg5lj4i 3 tcz dbyvyoiy34wz*ol 2c9) ,elow represents the -R group in the molecule belowlovbjw3, 4y29 z z4 tc*id)c oyig53yl?

1.Draw a diagram of a generalised amino acid, and label the functional groups. n5rd9y( c (knl

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 coi/1pze11p0xzl;k-7o p.a*w visml na h +pxs+rrect 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 prn1s5ers 4 fr) t:qr3zv ;tdq dfb/6ed,oteins influence the role they play within the body. The diagram below shows an integralnzq5t/db1sd r ;3evr ,:rtqesfd4f 6) 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.