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Topic B.4 · SL and HL

Proteins: notes and practice questions

Summary
  • This topic covers the fundamental structure, formation, and properties of proteins, which are essential macromolecules for all living organisms.
  • A generalized amino acid consists of a central alpha carbon atom bonded to an amine group -NH2\text{-NH}_2, a carboxyl group -COOH\text{-COOH}, a hydrogen atom, and a variable R-group.
  • Polypeptides are formed when amino acid monomers link together via peptide bonds in condensation reactions.
  • The vast diversity of proteins stems from the 20 different amino acids, their sequence, and the length of the polypeptide chain.
  • Essential amino acids are those that an organism cannot synthesize and must obtain from its diet.
  • Proteins can undergo denaturation, an irreversible change in their three-dimensional structure, typically caused by extreme temperatures or pH levels.

How it is examined

Drawing a generalized amino acid and a dipeptide are standard Paper 2 items and are marked strictly on group placement. HL work on the four bond types in tertiary structure is a classic 4-mark outline. Denaturation answers need the shape change, not just "the protein stops working".

Key ideas
  • B1.2.1 Generalized structure of an amino acid. Students should be able to draw a generalized amino acid showing the alpha carbon with amine group, carboxyl group, R-group and hydrogen attached.
  • B1.2.2 Condensation reactions forming dipeptides and longer chains. Students should be able to write the word equation and draw a generalized dipeptide after modelling the reaction with molecular models.
  • B1.2.3 Dietary requirements for amino acids. Essential amino acids cannot be synthesized and must come from food; non-essential ones can be made from other amino acids. Vegan diets need attention to essential amino acid intake.
  • B1.2.4 Infinite variety of possible peptide chains: 20 amino acids are coded for in the genetic code, chains can be any length from a few to thousands, and amino acids can be in any order. Be familiar with examples of polypeptides.
At HL
  • B1.2.6 Chemical diversity in the R-groups of amino acids as the basis for diversity in protein form and function. R-groups determine the properties of assembled polypeptides; they are hydrophobic or hydrophilic, and hydrophilic ones are polar or charged, acidic or basic.
  • B1.2.7 Impact of primary structure on the conformation of proteins. Sequence and the precise position of each amino acid determine the three-dimensional shape, so proteins have precise, predictable and repeatable structures.
  • B1.2.8 Pleating and coiling of secondary structure, with hydrogen bonding in regular positions stabilizing alpha helices and beta-pleated sheets.
  • B1.2.9 Dependence of tertiary structure on hydrogen bonds, ionic bonds, disulfide covalent bonds and hydrophobic interactions. Amine and carboxyl groups in R-groups can become charged by binding or dissociating hydrogen ions and then take part in ionic bonding.

Guiding questions

  • What is the relationship between amino acid sequence and the diversity in form and function of proteins?
  • How are protein molecules affected by their chemical and physical environments?

Linking questions

  • How do abiotic factors influence the form of molecules?
  • What is the relationship between the genome and the proteome of an organism?

Practice questions

9 questions · 2 easy · 4 medium · 3 hard
Showing 9 of 9

Question 1

EasyPaper 1A · calculator1 mark

Which of the following molecules contain the element nitrogen?

I. A triglyceride

II. An amino acid

III. A monosaccharide

A. I only

B. II only

C. I and II only

D. II and III only

Question 2

MediumPaper 1B · calculator6 marks
(a)

An experiment was conducted to investigate the effect of light intensity and temperature on the rate of photosynthesis in the aquatic plant Cabomba caroliniana. The rate of photosynthesis was measured by the volume of oxygen produced per minute. The results are shown in the graph below.

Graph showing the rate of photosynthesis (mm³ O₂ min⁻¹) on the y-axis from 0 to 10, and light intensity (arbitrary units) on the x-axis from 0 to 80. There are three curves representing different temperatures: 15 °C (circles), 25 °C (squares), and 35 °C (triangles). All curves start at the origin and increase with light intensity before plateauing. The 15 °C curve plateaus at the lowest rate (around 4.0 mm³ O₂ min⁻¹). The 35 °C curve plateaus at a higher rate (around 8.2 mm³ O₂ min⁻¹). The 25 °C curve plateaus at the highest rate (around 9.2 mm³ O₂ min⁻¹).

(a) State the rate of photosynthesis at a light intensity of 40 arbitrary units and a temperature of 25 °C.

[1]
(b)

(b) Identify the limiting factor for photosynthesis at a light intensity of 20 arbitrary units.

[1]
(c)

(c) Explain the effect of increasing the temperature from 15 °C to 25 °C on the rate of photosynthesis at a light intensity of 70 arbitrary units.

[2]
(d)

(d) The experiment was repeated at 45 °C. Predict, with a reason, the effect on the rate of photosynthesis at high light intensity compared to the rate at 35 °C.

[2]

Question 3

HardPaper 2 · calculator10 marks
(a)

The following table shows the mass of the nine essential amino acids in maize protein and kidney bean protein. The table also shows the percentage of the World Health Organization (WHO) recommended daily requirement that would be met if the recommended total daily amount of protein consumed was entirely maize or kidney bean protein.

Amino acidMaize (grain)Kidney bean (legume)
mg per g protein% of WHO amountmg per g protein% of WHO amount
Histidine28187%28187%
Isoleucine35117%43143%
Leucine120203%80136%
Lysine2556%65144%
Methionine30136%1150%
Phenylalanine45118%55145%
Threonine35152%40174%
Tryptophan583%10167%
Valine45115%50128%

Explain why certain amino acids are classified as essential in the human diet.

[2]
(b)(i)

Deduce, using the data, whether the WHO recommended daily intake is the same for all essential amino acids.

[2]
(b)(ii)

Suggest why the human body requires a greater mass of leucine than tryptophan in the diet.

[2]
(b)(iii)

Identify the amino acid that is required in the smallest quantity according to the WHO recommendations.

[1]
(c)

Justify the conclusion that relying solely on kidney beans for dietary protein could lead to a deficiency disease.

[1]
(d)

Discuss how a diet consisting entirely of plant-based foods can provide all essential amino acids, using the data provided.

[2]

Question 4

EasyPaper 1A · calculator1 mark

The table shows examples of essential and non-essential amino acids for humans.

Essential amino acidsNon-essential amino acids
methionineaspartic acid
tryptophanglutamic acid

Which statement is correct?

A. Methionine can be synthesized by human cells.

B. Aspartic acid must be absorbed from digested food.

C. Tryptophan cannot be synthesized by the human body.

D. Glutamic acid is not required for polypeptide synthesis.

Question 5

MediumPaper 2 · calculator5 marks
(a)

(a) The optimum pH for pepsin, an enzyme in the human stomach, is 2.0. The optimum pH for trypsin, an enzyme in the small intestine, is 8.0.

Calculate the ratio of the proton concentration at the optimum pH of pepsin to the proton concentration at the optimum pH of trypsin.

[2]
(b)

(b) Calculate the ratio of the proton concentration in a lysosome at pH 5.0 to the proton concentration in the surrounding cytoplasm at pH 7.2.

[2]
(c)

(c) State the term used to describe the irreversible change in the three-dimensional structure of an enzyme when exposed to a pH far outside its range of tolerance.

[1]

Question 6

HardPaper 2 · calculator15 marks
(a)

Proteins are highly diverse macromolecules that perform a wide range of functions in living organisms, including acting as biological catalysts.

Outline how the sequence of amino acids in a polypeptide is determined and how this leads to the vast diversity of proteins.

[4]
(b)

Enzymes are globular proteins that act as biological catalysts. Outline the effects of temperature and pH on the rate of enzyme-catalyzed reactions.

[4]
(c)

Explain the mechanism of enzyme action and how metabolic pathways can be controlled by feedback inhibition, using the synthesis of isoleucine as an example.

[7]

Question 7

MediumPaper 1A · calculator1 mark

A student is analyzing the nutritional content of a strictly plant-based diet. Why must the diet include a variety of different plant protein sources?

A. Plant proteins do not contain peptide bonds.

B. Individual plant sources may lack one or more essential amino acids.

C. Plant proteins are denatured more easily than animal proteins.

D. Plant proteins are composed of a different set of 20 amino acids than animal proteins.

Question 8

HardPaper 2 · calculator15 marks
(a)

(a) Outline the processes and conditions required for the spontaneous origin of cells on early Earth.

[4]
(b)

(b) Describe the advantages of compartmentalization in eukaryotic cells.

[4]
(c)

(c) Explain how the structure of proteins allows them to perform diverse functions in cell membranes and metabolism.

[7]

Question 9

MediumPaper 1A · calculator1 mark

Researchers recently determined the precise three-dimensional structure of the spike protein from a novel virus. To achieve this high-resolution image, they rapidly cooled the protein sample to −196 ∘C-196\text{ }^\circ\text{C} to prevent the formation of damaging water crystals, keeping the protein molecules stable in their natural conformation.

Which technique did the researchers use?

A. Cryogenic electron microscopy

B. Freeze-fracture electron microscopy

C. X-ray diffraction

D. Immunofluorescence

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What does Proteins cover in IB Biology?

This topic covers the fundamental structure, formation, and properties of proteins, which are essential macromolecules for all living organisms. A generalized amino acid consists of a central alpha carbon atom bonded to an amine group -NH_2, a carboxyl group -COOH, a hydrogen atom, and a variable R-group. Polypeptides are formed when amino acid monomers link together via peptide bonds in condensation reactions.

Is Proteins SL or HL?

Both. SL and HL students study Proteins, and HL goes further: B1.2.6 Chemical diversity in the R-groups of amino acids as the basis for diversity in protein form and function. R-groups determine the properties of assembled polypeptides; they are hydrophobic or hydrophilic, and hydrophilic ones are polar or charged, acidic or basic.

How do I revise Proteins for IB Biology?

Start from the core idea: this topic covers the fundamental structure, formation, and properties of proteins, which are essential macromolecules for all living organisms. In the exam: drawing a generalized amino acid and a dipeptide are standard Paper 2 items and are marked strictly on group placement. HL work on the four bond types in tertiary structure is a classic 4-mark outline. Then practise exam-style questions, easiest first, writing out every step of your working before you check it.

How does FourtyFive help me practise Proteins?

FourtyFive has 9 Proteins questions. Every answer you write is marked mark by mark, IB-style, and you see where each mark was won or lost. Every part has a hint, the AI tutor helps you through the step you are stuck on, and your Study Profile picks what to practise next.

Is FourtyFive free for Proteins practice?

Yes. A free account gives you 50 marked answers a month, and you do not need a card to sign up.

Can I handwrite Proteins answers on an iPad?

Yes. In the FourtyFive iPad app you write your working by hand with Apple Pencil, the way you would on paper, and it is marked the same way.

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