The amino acid distribution and residue-residue contacts in molecular chape
rones are different when compared to normal globular proteins. The study of
molecular chaperones reveals a different surrounding environment to exist
for the residues Cys, Trp, and His which may play an important role in dete
rmining the chaperone structures. Unlike globular proteins, it has been obs
erved that a one-to-one correspondence between the amino acid distribution
in a sequence and the structures of molecular chaperones. The preference of
amino acid residues surrounding all 20 types of residues in secondary stru
ctures and their accessible surface areas have been analysed.