Protein Structure Flashcards
What are all proteins made up of?
Polymers of amino acids
How many types of amino acids are there?
20 different amino acids
How many different amino acids can plants make?
Plants can make all 20 types of amino acids whereas animals can only make some. They obtain others through their diet.
What is the general structure of an amino acid?
Amine group -NH2
Carboxylic acid group -COOH
Hydrogen -H
Residual group
How is a dipeptide formed?
Two amino acids monomers undergo a condensation reaction. A peptide bond forms between the two units producing a dipeptide and a water molecule.
What is the primary structure of a protein?
Many amino acid molecules are joined together by peptide bonds during condensation reactions.
This creates a long chain of amino acids called a polypeptide chain.
A protein is made up of one or more polypeptide chains.
What reaction can break the peptide bond?
Hydrolysis reaction
Water reacts with the joined amino acids.
Functions of proteins
Hormones
Enzymes
Antibodies
Components of cell membranes
What are the two structures made in the secondary structure of a protein?
Alpha Helix
Beta pleated sheet
One protein may contain both structures or one.
What bonds are formed in a alpha helix structure?
Where do they form?
Hydrogen bonds form between the NH (amine group) and the C=O (carboxylic acid.
The H bonds stabilise the helix shape.
What bonds are formed in a beta pleated sheet structure? Where do they form?
Hydrogen bonds hold parallel chains between several polypeptide chains.
The type of bonding in the tertiary structure of the protein is dependent on…
The r-groups within the polypeptide chains
What chemical bonding occurs in the tertiary structure?
Disulphide bridging - Sulphur R groups
Ionic bonding - Between ionised R groups
Hydrogen bonding- alpha helix and beta pleated sheet
The chemical bonding in the tertiary structure work to..
Polypeptide chains bend and fold to give a precise 3D shape.
What maintains the final tertiary structure of the protein?
Chemical bonds and the hydrophobic interactions between the R groups