Protein Structure Levels Flashcards
How many different levels can proteins take?
4 different levels
What are the 4 different levels of protein structure?
Primary, Secondary, Tertiary and Quarternary
Describe a primary protein structure
Linear sequence of amino acids
What are the 3 secondary structures for proteins?
- α - helix
- β - pleated sheet
- Random coil
Describe α - helix secondary protein structure
- Spiral shaped amino acid chain fortified by weak hydrogen bonds
- Elastic in nature (can be stretched). returns to original shape after being stretched.
Describe β - pleated sheet secondary protein structure
- Triangular patterned amino acid chain fortified by weak hydrogen bonds.
- Represented through directional arrows.
- Cannot be stretched (already fully extended)
Describe Random coil secondary protein structure
- Irregular shaped amino acid chain fortified by weak hydrogen bonds.
- It is most active region of molecule.
Describe structure of tertiary proteins
Tertiary proteins have a unique shape consisting of primary and secondary amino acid chain sections
Describe Structure of Quarternary Proteins
Multiple chains of amino acids (tertiary groups) joining together to form a larger unique shaped protein
Which structure levels are non-functional (unpurposeful)
Primary and Secondary structure levels
Which structure levels are functional (purposeful)
Tertiary and Quarternary structure levels
What are the 4 types of bonds/interactions found in tertiary and quarternary structures?
- Hydrogen Bonds
- Ionic Bonds
- Disulphide bridges
- Interactions between hydrophobic and hydrophilic R groups
What is the purpose of these bonds found within tertiary and quaternary structures?
To help the protein maintain it’s structure and give the shape stability
What is a prosthetic group?
A group that is part of a protein but is not made of amino acids
What is the importance of protein’s having a unique shape?
Each protein can fulfill it’s purpose due to it’s unqiue shape
How does a DNA mutation affect the creation of a protein?
Creates a non-functional protein
What determines the shape and folding of proteins?
The properties of the functional groups found on the amino acids
Which amino acids generally face inside and outside
Hydrophobic amino acids face inwards while hydrophilic amino acids face outwards
Which amino acids like to come closer towards each other during the folding process of proteins?
Hydrophobic proteins like to come towards each other. Acidic and Basic amino acids that hold polar charges also attract each other.
A prosthetic group forms what type of protein?
Conjugated Protein
What are peptides?
Linear sequences of amino acids shorter than 50 amino acids.
