OCR A-Level Biology B H422
The Developing Cell: Cell Division and Cell Differentiation
The Developing Individual: Meiosis, Growth and Development
The Development of Species: Evolution and Classification
Cells and Microscopy
Water and Its Importance in Plants and Animals
Proteins and Enzymes
Nucleic Acids
Patterns of Inheritance
Population Genetics and Epigenetics
Gene Technologies
The Principles and Importance of Homeostasis
The Hormonal Control of Blood Glucose and the Management of Diabetes
Kidney Functions and Malfunctions
The Cellular Basis of Cancer and Treatment
Respiratory Diseases and Treatment
Cellular Respiration
Metabolism and Exercise
Pathogenic Microorganisms
The Immune System
Controlling Communicable Diseases
Photosynthesis, Food Production and Management of the Environment
The Impact of Population Increase
Planning and Implementing Practical Work
Analysing and Evaluating Practical Results
Practical Skills, Apparatus and Techniques
Fertility and Assisted Reproduction
The Effects of Ageing on the Reproductive System
Plant Reproduction
The Nervous System and the Identification and Consequences of Damage
Monitoring Visual Function
The Effect of Ageing on the Nervous System
The Heart and Monitoring Heart Function
Transport Systems in Mammals
Gas Exchange in Mammals and Plants
Proteins and Enzymes
Globular protein structure: enzymes and haemoglobin
- 3 things to know
- Components 01, 02 and 03
Overview
Recall questions on primary, secondary, tertiary and quaternary protein structure, the bonds including disulfide bridges that hold it, haemoglobin and its haem prosthetic group, the features and solubility of globular proteins, and denaturation.
What you need to know
Answer each one before you reveal it.
Name four types of interaction that hold a tertiary structure together.
What is a prosthetic group, and which one does haemoglobin contain?
Questions from this subtopic
Each one with the model answer underneath.
- 1
What is meant by the primary structure of a protein?
Model answer
It is the sequence of amino acids in the polypeptide chain, joined by peptide bonds.
- 2
What is the secondary structure of a protein?
Model answer
It is the regular local folding of the polypeptide backbone into an α-helix or a β-pleated sheet, held in place by hydrogen bonds between the C=O group of one amino acid and the N−H group of another.
- 3
What is meant by the tertiary structure of a protein?
Model answer
It is the overall three-dimensional shape into which the whole polypeptide folds, produced by interactions between the R groups of amino acids that may lie far apart in the primary sequence.
- 4
Name four types of interaction that hold a tertiary structure together.
Model answer
Hydrogen bonds, ionic bonds between charged R groups, hydrophobic interactions between non-polar R groups, and disulfide bridges.
- 5
Between which amino acid residues do disulfide bridges form, and why are they significant?
Model answer
They form between the sulfur-containing R groups of two cysteine residues, and because they are covalent they are much stronger than the other interactions and make the tertiary structure especially stable.
- 6
What is meant by quaternary structure?
Model answer
It is the arrangement of two or more separate polypeptide chains, together with any prosthetic group, into a single functional protein molecule.
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