Premium
Helix → β conformational transition of poly( L ‐lysine) on dye binding
Author(s) -
Scaria P. V.,
Atreyi M.,
Rao M. V. R.
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360251212
Subject(s) - chemistry , cooperativity , cooperative binding , lysine , helix (gastropod) , side chain , aqueous solution , conformational change , benzene , stereochemistry , amino acid , transition (genetics) , binding site , polymer chemistry , crystallography , organic chemistry , biochemistry , polymer , ecology , snail , gene , biology
Binding of an azo dye, 4′‐dimethyl amino azo benzene‐4‐carboxylic acid (DAAC) to poly( L ‐lysine) (PLL) in basic aqueous solutions at 20°C has been studied. The azo dye was found to bind to PLL when its side‐chain amino groups are in the uncharged state. This was found to be a cooperative phenomenon, and the binding constant and cooperativity factor have been evaluated. The binding of the dye was found to result in a conformational transition of PLL from the α‐helix to the β‐sheet, which in turn helps in increased dye binding.