WJEC A-Level Chemistry 1410QS
Formulae and Equations
Basic Ideas About Atoms
Chemical Calculations
Bonding
Solid Structures
The Periodic Table
Simple Equilibria and Acid-Base Reactions
Thermochemistry
Rates of Reaction
The Wider Impact of Chemistry
Organic Compounds
Hydrocarbons
Halogenoalkanes
Alcohols and Carboxylic Acids
Instrumental Analysis
Redox and Standard Electrode Potential
Redox Reactions
Chemistry of the P-Block
Chemistry of the D-Block Transition Metals
Chemical Kinetics
Enthalpy Changes for Solids and Solutions
Entropy and Feasibility of Reactions
Equilibrium Constants
Acid-Base Equilibria
Stereoisomerism
Aromaticity
Alcohols and Phenols
Aldehydes and Ketones
Carboxylic Acids and Their Derivatives
Amines
Amino Acids, Peptides and Proteins
Organic Synthesis and Analysis
Practical Skills and Techniques
Planning, Analysis and Evaluation
Core Experiments and Their Chemistry
Mathematical Skills in Chemistry
Amino Acids, Peptides and Proteins
Levels of protein structure and the bonds that hold them
- 3 things to know
- A2 Unit 4
Overview
Recall questions on primary structure of a protein and tertiary structure of a protein.
What you need to know
Answer each one before you reveal it.
Why is the polypeptide backbone able to form hydrogen bonds at all?
Why does a large change in pH denature a protein?
Questions from this subtopic
Each one with the model answer underneath.
- 1
What is meant by the primary structure of a protein?
Model answer
The primary structure is the order in which the amino acid residues are joined along the polypeptide chain, read from the free amine end to the free carboxyl end. It says nothing about shape, only about sequence.
- 2
Which type of bond holds the primary structure of a protein together?
Model answer
Covalent bonds, specifically the peptide (amide) links between successive residues. These are strong covalent bonds, which is why the sequence is not disturbed by moderate heating or by a change of pH.
- 3
What is meant by the secondary structure of a protein, and what two forms does it commonly take?
Model answer
Secondary structure is the regular, repeating way in which a local stretch of the polypeptide backbone arranges itself in space. The two common forms are the α-helix, a coiled spiral, and the β-pleated sheet, in which lengths of chain lie alongside one another in a folded sheet.
- 4
Which interaction holds an α-helix in shape, and between which atoms does it act?
Model answer
Hydrogen bonding holds the helix in shape. Each hydrogen bond forms between the slightly negative oxygen of a C=O group in one peptide link and the slightly positive hydrogen of an N−H group in a peptide link further along the same chain. The side chains are not involved; the bonding is between parts of the backbone.
- 5
How is a β-pleated sheet held together?
Model answer
Sections of the polypeptide backbone lie side by side, and hydrogen bonds form between the C=O group of a peptide link in one section and the N−H group of a peptide link in the neighbouring section. Many such hydrogen bonds acting together across the sheet make the arrangement stable.
- 6
Why is the polypeptide backbone able to form hydrogen bonds at all?
Model answer
Each peptide link contains an N−H group and a C=O group. Nitrogen and oxygen are both much more electronegative than hydrogen and carbon, so the hydrogen of N−H carries a δ+ charge and the oxygen of C=O carries a δ− charge and has lone pairs. A hydrogen atom bonded to nitrogen attracted to a lone pair on oxygen is a hydrogen bond.
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