Session 5.2a - Lecture 1 - Protein Folding and Protein Structure Review Flashcards
ILO
Review of protein structure
- Protein structure review
- Enzymes review (Session 6)
- AAs that make up proteins and their properties
Protein folding
- How do proteins actually fold
- How do they get their 3D shape
- Important interactions that help protein folding occur
Name the 4 layers of protein structure.
Primary structure
Secondary structure
Tertiary structure
Quaternary structure
Explain how the first 2 layers of protein structure are related.
The primary sequence folds to give a localised secondary sequence.
Give 2 examples of secondary structure conformations.
- Alpha helix
- Beta sheet or beta strands
What is the structure of alpha helix secondary structure?
- Helical shape
- Relatively compact
- H-bonds running up and down chain to stabilise it
- R groups on outside
What shape is the alpha helix secondary structure?
Helical and relatively compact
Where do the R groups lie in the alpha helix secondary structure?
On the outside
What is the structure of beta sheet/strand secondary structure?
- More extended conformation
- H bonds stabilise it
What stabilises the alpha helix and beta sheet secondary structures?
H-bonds
- running up and down chain in alpha helix
- between individual strands in beta strands
What is the tertiary structure of a protein?
Where parts of the molecule fold up, so parts that are from far apart in the original polypeptide sequence may be close together
How are some amino acids that are far apart in the original polypeptide sequence found close together in proteins?
Due to folding of the tertiary structure
What element of proteins do only some proteins contain?
Quaternary structure
What is quaternary structure?
Where there is distinct subunits - >1 subunit but we can also it could be interactions with macromolecules (big molecules, e.g. DNA, RNA) in other constituent elements.
Give 2 examples of macromolecules found in the human body.
DNA
RNA
Does myoglobin have quarternary structure?
No, it is monomeric, has 1 single polypeptide chain
Myoglobin can bind to a haem group. Does this mean it has quarternary structure?
No, because haem isn’t really a macromolecule so we don’t take that into account.
Give an example of a protein with quarternary structure.
Haemoglobin - made up of 4 subunits.
How many subunits is haemoglobin made up of?
4
Fig. 2
Label this image
Protein structure and function
Primary structure
Secondary structure
Tertiary structure
Quarternary structure
Draw the different layers of protein structure.
See Fig. 2
Protein structure and function
Primary structure
Secondary structure
Tertiary structure
Quarternary structure
What are the forces involved in maintaining protein structure in the primary sequence?
Covalent (peptide)
What are the forces involved in maintaining protein structure in the secondary sequence?
H-bonds
What are the forces involved in maintaining protein structure in the tertiary sequence?
- Covalent (disulphide)
- Ionic
- H-bonds
- van der Waals
- Hydrophobic
What are the forces involved in maintaining protein structure in the quaternary sequence?
- Covalent (disulphide)
- Ionic
- H-bonds
- van der Waals
- Hydrophobic