Friday, July 13, 2012

STPM Biology - chapter 1: Reision essay question 24


24. Explain the meaning of the terms primary structure, secondary structure, tertiary structure and quaternary structure of protein.

Answer:

Primary structure
-describes the type of amino acids and the specific linear sequence of amino acids in a polypeptide chains
-the sequence of amino acids of a protein dictates its biological function
-A substitution or deletion of even one amino acid can affect the structure and function of the protein.

e.g. lysozyme which consists of a single polypeptide chain of 129 amino acid residues. The enzyme causes lysis of the bacterial cell wall. It is found in many tissues and secretions of the human body, in plants and in egg whites.

Secondary structure
-the regular arrangement of the polypeptide chain
-coiled to form a right-handed α-helix
              α-helix
 *held together by hydrogen bonds between every fourth
*e.g. the fibrous protein keratin found in hair, nails, horn and feathers
-folded to form beta-pleated sheets
beta- pleated sheets
*the polypeptide chains lie parallel to one another and are held together by hydrogen bonds
*e.g. silk protein fibroin

>Many hydrogen bonds are formed between C=O and NH-groups from the peptide bond regions. These maintain the stable structure of α-helix and beta-pleated sheets.
>Sometimes certain regions of the polypeptide chain have no regular secondary structure and form a ‘random coil’.

Tertiary structure
-formed by the folding and coiling of the secondary structure of polypeptide chains to form a precise, compact globular protein which determines its function
-the compact three dimensional shape is maintained by hydrogen bonds, ionic bonds, hydrophobic interactions and Van der Waals interactions,
-e.g. enzymes, antibodies, protein hormones, and myoglobin, the oxygen-storage red pigments in muscles

Quaternary structures
-consist of two or more polypeptide chains joined to form a single functional molecule
e.g. the protein haemoglobin
 *red pigment found in red blood cells
 *made up of two α-chains and beta-chains
 *each polypeptide is coiled to form a globular tertiary structure with a haem group containing an iron ion
*the four chains are closely associated to produce the quaternary structure of protein
*the structure is maintained by weak hydrophobic interactions and Van der Waal interactions.
*a haemoglobin molecule

Assignment submitted by S.M., Kang, E.S., Ong, T.W., Tan 2011/2012 (IBM)




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