Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration.
J Mol Recognit
; 28(3): 125-8, 2015 Mar.
Article
em En
| MEDLINE
| ID: mdl-25615849
ABSTRACT
The association constant of a well-known streptavidin-biotin binding has only been inferred from separately measured kinetic parameters. In a single experiment, we obtained Ka 1 × 10(12) M(-1) by using a streptavidin-binding aptamer and ligand-displacement isothermal titration calorimetry. This study explores the challenges of determining thermodynamic parameters and the derived equilibrium binding affinity of tight ligand-receptor binding.
Palavras-chave
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Biotina
/
Calorimetria
/
Estreptavidina
/
Aptâmeros de Nucleotídeos
Idioma:
En
Revista:
J Mol Recognit
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
Taiwan