Analysis of hydrophobic and charged patches and influence of medium- and long-range interactions in molecular chaperones.
The amino acid composition of the aromatic residues Phe, Tyr and Trp are much less significant in chaperones and the residues Cys, Glu, His, Met and Pro vary significantly in chaperones compared to normal globular proteins. In the present work, we have analysed the hydrophobic and charged patches in molecular chaperones which provide more insight for a better understanding of chaperone folding. Also, we have investigated the role of medium- and long-range contacts in chaperones and the preference of amino acid residues influenced by these interactions. Furthermore, the role of hydrophobic and helix-forming residues and disulfide bonding in these interactions have been discussed.
Kumarevel
T S
TS
Department of Crystallography and Biophysics, University of Madras, Tamil Nadu, India.
Gromiha
M M
MM
Ponnuswamy
M N
MN
D000596:Amino Acids / Q000032:analysis; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding
D000596:Amino Acids; D018832:Molecular Chaperones