Proteins
Proteins have a variety of functions within all living organisms.
They are very large molecules (polymers) made up of amino acids (monomers)
General structures of an Amino Acids
Formation of Polypeptides
Can be repeated many times with amino acids being added to produce polypeptide chains which may contain thousands of amino acids
Hydrolysis will break up a polypeptide and release the amino acids. This happens in digestion
Primary structure
The sequence of amino acids held with peptide bonds
Secondary structure
The folding of the polypeptide chain:
>coiled to form an alpha-helix
>folded to form beta-pleated sheets
-Held with hydrogen bonds
Tertiary structure
This is the folding up of the alpha-helix to form a precise three-dimensional shape. Bonds may form between the R groups of the amino acids which find themselves close together. The shape is maintained by 4 types of bonds:
Quaternary structure
This is two or more polypeptides held together e.g. insulin has 2 chains, haemoglobin and antibodies have 4
-Held with hydrogen bonds
Fibrous proteins
-polypeptide chains don’t fold but remain as straight chains with several chains cross-linked (H bonds)
-secondary structure only - straight chains which can be linked by H bonds (quaternary structure)
-Insoluble
-Very stable and strong
Important for structures and strength e.g.
>tendons, skin - collagen
>hair, beaks, claws - keratin
>silk
>muscle contractile proteins
Globular proteins
Collagen
Fibrous protein found in skin and tendons. Provides strength and toughness
Made up of 3 polypeptide chains held with