Publication | Closed Access
Helix → β conformational transition of poly(<scp>L</scp>‐lysine) on dye binding
16
Citations
25
References
1986
Year
Macromolecular ChemistryEngineeringMolecular BiologyConformational TransitionPolymersCooperative PhenomenonProtein FoldingPolymer ChemistryBiophysicsProtein ChemistryBiochemistryConformational StudyDye BindingMacromolecular ArchitectureMolecular ModelingMacromolecular ScienceNatural SciencesPolymer ScienceAbstract BindingMacromolecular SystemMolecular Biophysics
Abstract 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.
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