Hierarchical Structures and Biology

 

Main Types of Biological Molecules

1.       Lipids (fats)

Fatty acids have a backbone of up to 36 carbon atoms and end with a –COOH group.   The carbon chains can have unsaturated bonds as well as saturated.


Triglycerides such as butter and lard, are the most abundant fats in the body and are its richest energy source.  They consist of 3 fatty acid tails attached to a glycerol molecule.  Again chains can be saturated or unsaturated.

 

 

 

 

Phospholipids also have a glycerol ‘backbone’, but the third attachment to the glycerol is a hydrophilic head consisting of a phosphate plus another hydrophilic group. 


 


e.g. Phosphatidylcholine – one of the commonest

 

Recall phospholipids are the main constituent of animal cell membranes in a double layer.

 

 

2 Nucleic Acids and DNA

Bonding is always A-T and C-G (base pairing), and the pairs are linked through a sugar phosphate backbone..

 

RNA has uracil in place of thymine.

3 Polysaccharides


Polysaccharides are long chains of simple sugar molecules. Sugars are 5 or 6 membered saturated carbon rings.

Polysaccharides are particularly important in plants.  Examples include starch and cellulose.

 

 

 

 

 

 

 

 

 

 

 

 


4 Proteins

 


Peptide bond forms with release of water.

 

Proteins vary hugely in size i.e. how many amino acids are strung together.

 

 

 

 

 

 

 

Proteins are not random coils.

They have very precise secondary structure, and this is vital for their function.

 

 

 

 

 

Protein Secondary Structure

 

Two commonly repeating motifs:


a helix

 


This is the most abundant type of secondary structure in proteins.

 

The helix has an average of 3.6 amino acids per turn with a hydrogen bond formed between C=O and N-H groups about every fourth residue.

 

Average length is 10 amino acids

b sheet

 

Again stabilised by hydrogen bonding, with neighbouring chains running parallel or antiparallel
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Hydrogen bonding forms between an average of 5-10 consecutive amino acids in one portion of the chain with another 5-10 further down the chain.

 

The interacting regions may be adjacent, with a short loop in between or far apart with other structures in between.

 

The tertiary shape of a protein is determined by the location of these standard motifs and how the chains pack in between. 

Shape determines function