There are two common types of secondary structure of proteins:

(i) α–helix structure

(ii) β–pleated sheet structure

α–Helix structure

If the size of R-groups is quite large then the intramolecular bonds are formed between the C=O of one amino acid and the N-H group of the forth amino acid residue in the chain. This causes the polypeptide chain to coil up into a spiral structure called righ handed α-helix structure.

β -pleated sheet structure

In this conformation, the polypeptide chains lie side by side in a zig0zag manner with alternate R groups on the same side situated at fixed distances apart. The two such neighbouring polypeptide chains are held together by interbounded to form a sheet. These sheets are then stacked one above the other like the pages of the book to form a 3-D structure. This structure resembles pleated folds of drapery and hence is called β–pleated sheet structure. The polypeptide chains can link together in parallel and anti-parallel sequence. Such sheet like structure can easily slip on each other. Proteins of this structure are soft.