Kinetic study of membrane protein interactions: from three to two dimensions.
Sci Rep
; 14(1): 882, 2024 01 09.
Article
em En
| MEDLINE
| ID: mdl-38195620
ABSTRACT
Molecular interactions are contingent upon the system's dimensionality. Notably, comprehending the impact of dimensionality on protein-protein interactions holds paramount importance in foreseeing protein behaviour across diverse scenarios, encompassing both solution and membrane environments. Here, we unravel interactions among membrane proteins across various dimensionalities by quantifying their binding rates through fluorescence recovery experiments. Our findings are presented through the examination of two protein systems streptavidin-biotin and a protein complex constituting a bacterial efflux pump. We present here an original approach for gauging a two-dimensional binding constant between membrane proteins embedded in two opposite membranes. The quotient of protein binding rates in solution and on the membrane represents a metric denoting the exploration distance of the interacting sites-a novel interpretation.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Biotina
/
Proteínas de Membrana
Idioma:
En
Revista:
Sci Rep
Ano de publicação:
2024
Tipo de documento:
Article