New Approach for Determination of Macroscopic Binding Constants of Ligands to Macromolecules
β Scribed by H Gharibi; M.A Safarpour; A.A Rafati
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 97 KB
- Volume
- 219
- Category
- Article
- ISSN
- 0021-9797
No coin nor oath required. For personal study only.
β¦ Synopsis
A new method has been developed for determining macroscopic binding constants of a few surfactants to some macromolecules. Then, the binding of ionic surfactants (cetyltrimethyl ammonium bromide, tetradecyltrimethyl ammonium bromide, and sodium tetradecyl sulfate) [STS]) to macromolecules (bovine serum albumin, human serum albumin, and polyvinyl pyrollidone was investigated. The binding constants and binding isotherms were calculated using this new method. Experimental data were obtained through a potentiometry technique. Finally, the results obtained were compared with the results obtained based on the Wyman binding potential concept.
π SIMILAR VOLUMES
The equilibrium constant for the binding of a spectroscopically invisible ligand to its protein receptor can be determined in a competition experiment, by using a structural analog that contains a reporter group (fluorophor). A novel mathematical treatment of the multiple equilibria allows the analy
Degradative transfer reactions for diphenylpicrylhydrazine (DPPH-H), 1,3-diphenylpropene (DPP), and fluorene (FLU) have been examined using styrene and methyl methacrylate as monomers. A new procedure has been followed, depending upon analyses of polymers for end groups derived from azobisisobutyron
## Abstract A new pulsed gradient spinβecho NMR diffusion sequence, PGSEβWATERGATE, which is based on the extremely efficient WATERGATE solvent suppression sequence, is presented. The sequence is simple to set up and particularly suited to measuring the diffusion coefficients of small ligands in aq