3.1.4.1 Protein Flashcards
Function of protein
Growth and repair
Enzyme
Hormones
In the cell membrane
Structural, protein, collagen
Antibodies in immune system
Transport in haemoglobin
Muscle contraction
What make a protein?
Carbon, hydrogen oxygen nitrogen
Some contain sulphur and phosphorus
General structure of protein
Amino group (H-N-H)
Variable group (H-C-R)
Carboxylic group (o=c-oh)
Polymerisation
Chain of many amino acid
Few chain of polypeptide form protein
Protein can be made up of one polypeptide chain or many
Biuret test
Add biuret reagent (sodium hydroxide and copper (ll) sulphate
Purple colour indicate presences of peptide bond there fore protein (negative result with blue solution will show if just prescience of amino acid )
Apparatus accurately measure the concentration of protein
Colorimeter
Explain how change in primary structure of a globular protein may result in a different 3-D structure
sequence of amino acid will be change in primary structure
The place where hydrogen bond together, it’s different
So it is fold/ coiled in a different way
Tertiary structure change
Four level of protein
Primary
Secondary
Tertiary
Quaternary
Primary structure
The sequence of amino acid
Secondary structure
The primary structure is put into the secondary structure by hydrogen bond between nearby oxygen and hydrogen forming alpha helix or beta platted sheet
Tertiary structure
R group interaction pulls the secondary structure into a more complex 3D shape.
Ionic bond (opposite charge ions)
Disulfide bond
Hydrogen bond
Hydrophobic interactions
Hydrophilic interaction
Quaternary structure
Two or more peptide chain bond together
Prosthetic group ( non protein ) may also be present
E.g iron in haemoglobin
Example of protein
Haemoglobin
Collagen
Enzyme
Explain Haemoglobin
- quaternary
- globular protein
- metabolic role
- soluble in water
- spherical shape
Explain collagen
In fibrous tissue (tendons join muscle to bone)
Structural role
Insoluble in water
Form fibre
Triple helix
Exam Q : full description of structure of protein
Polymer of amino acid
joined by peptide bond
formed by condensation
primary structure is order/ sequence of amino acid
Secondary structure is folding of polypeptide chain due to hydrogen bonding
Tertiary structure is 3D folding due to hydrogen bond, ionic and disulphide bridges
Quaternary structure is 2 or more polypeptide chain