Describe the structure of an amino acid. (F)
State how many amino acids occur in life.
20
Explain how the variety of amino acids leads to a wide range of dipeptides and very quickly to an incredible variety of polypeptide chains.
Define the term “polypeptide chain”.
Chain of three or more amino acids
Describe how one end of a polypeptide chain differs from the other end.
One end is an amine group (-NH2) which has basic properties, and the other end is a carboxyl group (-COOH) and has acidic properties.
Define the term “primary structure” of a protein. (F)
The sequence of amino acids.
Define the term “secondary structure” of a protein and describe the two different types. (F)
The folding of the polypeptide chain into an alpha helix (coiled) or beta pleated sheet (flat).
Define the term “tertiary structure” of a protein. (F)
The 3D shape of a polypeptide chain.
Explain how the primary structure of a protein determines its tertiary structure.
The R-groups on the amino acids affect the bonding in the tertiary structure.
Define the term “quaternary structure” of a protein.
When two or more polypeptides associate.
Define the term “globular protein”. (F)
Spherical, water-soluble protein.
Define the term “prosthetic group”. (F)
Non-protein component of a conjugated protein
Give an example of a conjugated protein (the bloody one).
Haemoglobin
Give an example of an enzyme (the H2O2 one ;) ).
Catalase
Give an example of a peptide hormone (the sugary one).
Insulin
Give 3 examples of fibrous proteins.
Describe the structure of collagen.
Describe the structure of keratin.
- disulfide bridges (degree of disulfide bonds determines flexibility)
Describe the structure of elastin.
- covalent bonds between lysine amino acids
Compare the structure of globular and fibrous proteins.
- F is long
Compare the properties of globular and fibrous proteins.
- F is insoluble
Compare the functions of globular and fibrous proteins.
- F acts as structural components
Identify the key structural components of haemoglobin.
State the properties of haemoglobin.
Haem group combines reversibly with an oxygen molecule