Syllabus Edition

First teaching 2014

Last exams 2024

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Proteins (DP IB Biology: SL)

Topic Questions

3 hours35 questions
1a1 mark

The image below shows the amino acid histidine.

e-1a

Circle the section of the amino acid that is unique to histidine. 

1b1 mark

State the type of reaction that occurs when two amino acids bond with each other. 

1c1 mark

The image shows two histidine amino acids with the diagrams not fully complete. 

Complete the image to include the structure of a peptide bond joining the two amino acids together into a dipeptide.

e-1c

1d1 mark

In a polypeptide with 100 amino acids, how many peptide bonds exist within the chain? 

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2a2 marks

The protein Rubisco is an enzyme. 

What is the function of the enzyme Rubisco in living organisms? 

2b1 mark

Enzymes have a specific three-dimensional conformation that enables them to carry out their roles in living organisms. 

Which part of the amino acid determines the conformation of the protein?

2c2 marks

In certain conditions, such as high temperatures, the 3D conformation of proteins can be lost. 

(i)
What is the scientific name given to when a protein loses its 3D conformation? 

[1]

(ii)
State one condition, other than temperature, that can cause the 3D conformation of a protein to be lost. 

[1]

2d2 marks

Sketch a graph to show how the rate of reaction of Rubisco changes over a range of temperatures. 

Use the axes provided below.

e-2d

[2]

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3a1 mark

What is the name of the part of the cell where polypeptide synthesis takes place?

3b3 marks

When a polypeptide is synthesised it is important that the amino acids are combined in the correct order to produce a functional protein.

Outline the process that allows the amino acids to be added to the polypeptide in the correct order. 

3c3 marks

After a polypeptide has been synthesised it must undergo a series of changes before it can become a functional protein.

Describe the changes that occur between polypeptide synthesis and the formation of the functional protein. 

3d2 marks

How might a change in the DNA affect the way that the process of protein folding occurs? 

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4a1 mark

What is meant by the term proteome?

4b2 marks

There are two main categories of proteins: globular and fibrous. 

The protein insulin is a hormone.

State whether insulin is a globular or a fibrous protein, and give a reason for your choice. 

4c2 marks

The image below shows the structure of collagen at various levels of detail. 

collagen-sq

Use the image to suggest two features of collagen that enable it to be a strong, structural protein. 

4d
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3 marks

One of the polypeptide chains that forms a molecule of collagen contains 1049 peptide bonds.

Assuming all the chains that form collagen are identical in length, how many amino acids would be found in a single molecule of collagen?

Explain your answer. 

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5a3 marks

One mark is available for clarity of communication throughout this question. 

Every individual has a unique proteome.

Explain how this is possible. 

5b4 marks

Describe the process of protein denaturing. 

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1a2 marks

The diagram below shows the structure of a commonly-occurring amino acid in nature.

LBKVbIpM_q1a-2-3-proteins-medium-ib-hl-biology-sq

Identify the word that best describes the chemical nature of this amino acid's R group from the following list: saturated; hydrophobic; acidic; aromatic. Give a reason for your answer.

1b2 marks

Nine of the twenty amino acids are described as 'essential amino acids' for humans.

Define and explain the term, 'essential' in this context.

1c3 marks

The amino acid alanine has a single methyl group (-CH3) as its R group.

Draw the dipeptide formed when two alanine molecules join together.

1d2 marks

Calculate the number of combinations of the 20 commonly-occurring amino acids that can be joined together in a short polypeptide chain of 8 amino acids in length, in which each amino acid is different to the other seven.

Give your answer to 1 significant figure.

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2a3 marks

Explain how the amino acid sequence determines the three-dimensional conformation of a polypeptide.

2b2 marks

Calculate, in pairs of nucleotides, the total length of a gene that codes for a polypeptide of 351 amino acids in length. In this gene, 40% of its DNA is non-coding.

2c3 marks

Distinguish between the structures and properties of collagen and haemoglobin.

2d2 marks

In cell membranes, proteins can be positioned within the phospholipid bilayer, in order to perform various functions. Some membrane proteins can span the entire bilayer as shown in the diagram below.q2d-2-3-proteins-medium-ib-hl-biology-sqExplain why the amino acids in region B of the membrane protein tend to have hydrophobic R groups towards the surface, whilst those in regions A and C tend to have hydrophilic R groups towards their surfaces.

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3a2 marks

The image below shows the process of denaturation of a polypeptide.q3a-2-3-proteins-medium-ib-hl-biology-sq

Describe one change of conditions that can lead to such a denaturation and the effect this change has on the polypeptide's structure.

3b4 marks

Use your knowledge of the denaturation of proteins to explain the nutritional benefits of cooking protein-rich food like eggs before eating them.

3c1 mark

The proteins of many different extremophile prokaryotes have been studied extensively. A common feature among these proteins is a more tightly-packed hydrophobic core that prevents denaturation at high temperature or extremes of pH.

Suggest one benefit of humans developing detailed knowledge of these proteins and their structures.

3d2 marks

State the source and the property of the enzyme Taq polymerase that allows it to be used in the Polymerase Chain Reaction when amplifying small amounts of genetic material.

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4a3 marks

Following partial hydrolysis of a naturally-occurring protein, samples of the polypeptides that were produced were identified.

Select from the table below the two molecular formulas that could be one of the naturally-occurring polypeptides.

Give reasons for your answer.

Polypeptide Number Number of amino acids long Molecular formula
I. 12 C30H54N10O33S4
II. 44 C66H86O78N59S3
III. 6 C18H26O18N12
IV. 37 C60H102O75N42S15
4b1 mark

Identify the role that proteins play in the central dogma of gene expression.

4c2 marks

A protein found in leaves is thought to be the most abundant protein in nature.

State its name and describe its basic function. 

4d3 marks

Explain why the genome of an organism is fixed, whereas the organism's proteome can vary.

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5a3 marks

One mark is available for clarity of communication throughout this question.

Use your knowledge of protein structure to explain the term, 'specificity' in the context of immunoglobulins and their mode of action.

5b4 marks

Outline, with examples, the main roles that proteins play in organisms.

5c8 marks
For each of the proteins listed A - D below, state one aspect of its structure and one function that is enabled by the structural feature that you have stated.

  1. Ribulose Bisphosphate Carboxylase (RuBisCo)
  2. Spider silk
  3. Immunoglobulins
  4. Rhodopsin

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1a
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3 marks

Albumin is a protein found in the plasma of the blood. 

Albumin transports hormones, fatty acids, and other compounds in the blood, buffers blood pH, and maintains oncotic pressure, among other functions.

The gene that codes for human albumin is 16,961 DNA bases long. The protein is made up of 585 amino acids. 

Calculate the ratio of non-coding to coding DNA in the albumin gene.

1b3 marks

Albumin is a protein that can be found in a range of vertebrate species.

Different species have slight variations in the structure of the protein. For example, bovine (cow) albumin has 583 amino acids. 

Cows and humans share a common ancestor. 

Suggest why it is the case that the two types of albumin are similar, but not completely the same as each other. 

1c4 marks

Egg whites are mostly made of albumin.

When the albumin in egg white becomes denatured it causes the 'white' to change from being colourless to being opaque white.

A student wanted to investigate how temperature affects the denaturing of albumin. 

Outline a method that the student could use in order to carry out this investigation. 

1d2 marks

When the albumin in the egg white is not denatured it is soluble in the liquid, however, when it denatures it becomes insoluble. This is the mechanism that causes the colour change. 

Explain how the protein can have different properties before and after denaturing. 

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2a
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2 marks

A theoretical polypeptide chain is 26 amino acids long. 

Calculate how many different possible combinations of amino acids could exist within this chain. 

Give your answer in standard form. 

2b2 marks

An average sized polypeptide of around 400 amino acids in length is said to have an infinite number of possible amino acid combinations. 

Explain why it is possible for such a vast variety of polypeptides to exist. 

2c1 mark

In some rare circumstances, some organisms have been found to contain unusual amino acids that are not shared with the majority of other organisms. 

Selenocysteine is one of them, and is shown in the image below. h-2c

   

Using the image, state what makes selenocysteine so unusual compared to other amino acids. 

2d3 marks

Some amino acids exist that have been man-made in a lab and have never been used naturally in the proteins of living organisms. 

Describe the features that must exist in these molecules in order for them to be classified as amino acids. 

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3a2 marks

Insulin is a protein that is produced naturally by most people, however, people with insulin-dependent diabetes rely on injecting insulin to replace the protein that they cannot produce for themselves. 

Explain why the insulin must be injected into the blood instead of taken orally. 

3b2 marks

Many years ago, insulin used to be taken from cows and pigs to treat people with diabetes. 

Using your knowledge of protein structure, suggest why pig and cow insulin was less effective at regulating blood glucose levels than human insulin. 

3c3 marks

In modern medicine, human insulin is secreted from genetically modified bacteria into large industrial vats called fermenters. This allows the insulin to be extracted and purified for human use.

Outline why the insulin produced by the genetically modified bacteria is identical to insulin produced by a human.

3d5 marks

Other organisms that can be genetically engineered to produce proteins for human medicine are goats.

Goats can be engineered to produce protein in their milk, for example, a protein called ATryn, which is used to reduce the risk of blood clots in human patients.

The goats can be milked and then the protein is extracted to be given to patients.

Compare and contrast this method of producing proteins for human medicine to the use of genetically modified bacteria for the same purpose.

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4a3 marks

Haemoglobin is an example of a protein. 

Using the diagram below and your own knowledge, describe the structure of haemoglobin.

h-4a

4b3 marks

During a human's lifetime, they use different forms of haemoglobin. 

Fetal haemoglobin varies in structure to normal haemoglobin and it is adapted to absorb oxygen when the oxygen concentration is lower. 

Why would this benefit the foetus?  

4c2 marks

Foetal haemoglobin is phased out quite early on in development and is replaced with adult haemoglobin. 

This is an example of how the proteome changes throughout an individual's lifetime.

Unlike the proteome, the genome remains fixed. 

Outline how it is possible for the proteome to vary throughout an individual's lifetime, even though the genome stays the same.

4d3 marks

The image below shows the part of haemoglobin that binds to oxygen to deliver it around the body. 

Is this an amino acid? Explain your reasoning. 

haemoglobin

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5a3 marks

One mark is available for clarity of communication throughout this question. 

State the essential properties of membrane-bound proteins.

5b5 marks

Explain why studying the proteomes of a variety of different species is beneficial to humans. 

Use specific examples in your answer. 

5c7 marks

If a person has been infected with the influenza virus in the past they possess the necessary immunoglobulins to provide immunity to that virus again in the future. 

Influenza viruses contain RNA as their genetic information. 

State, with reference to RNA and protein structure, why it is possible for people to get the flu several times in their life. 

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