Spatial constraints and group behaviour in globular proteins.

A comparative analysis has been attempted on the spatial placement of amino acid residues derived from radial, ellipsoidal and exposure arrangements. The group behaviour of residues and their restraining influence in protein folding have been brought out. A study is also made on the geometry of proteins, the exposure arrangement of residues and the spatial distribution of the physical properties of the residues in globular proteins. It has been shown that the group constraints along with the information on the shape of the globular proteins would be highly useful in assigning the spatial and exposure arrangements of residues in globular proteins.