Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.
Biochim Biophys Acta
; 1838(1 Pt A): 56-68, 2014 Jan.
Article
en En
| MEDLINE
| ID: mdl-23603221
Membrane proteins are embedded in lipid bilayers and facilitate the communication between the external environment and the interior of the cell. This communication is often mediated by the binding of ligands to the membrane protein. Understanding the nature of the interaction between a ligand and a membrane protein is required to both understand the mechanism of action of these proteins and for the development of novel pharmacological drugs. The highly hydrophobic nature of membrane proteins and the requirement of a lipid bilayer for native function have hampered the structural and molecular characterizations of these proteins under physiologically relevant conditions. Atomic force microscopy offers a solution to studying membrane proteins and their interactions with ligands under physiologically relevant conditions and can provide novel insights about the nature of these critical molecular interactions that facilitate cellular communication. In this review, we provide an overview of the atomic force microscopy technique and discuss its application in the study of a variety of questions related to the interaction between a membrane protein and a ligand. This article is part of a Special Issue entitled: Structural and biophysical characterization of membrane protein-ligand binding.
Palabras clave
AFM; DFS; Energy landscape; Force spectroscopy; FD; G protein-coupled receptor; GPCR; HOPG; ICAM-1; Imaging; LFA-1; LHRH; Molecular interaction; PE40; Protein structure; Pseudomonas aeruginosa exotoxin 40; SMFS; STM; atomic force microscopy; dynamic single-molecule force spectroscopy; forcedistance; highly ordered pyrolytic graphite; intercellular adhesion molecule-1; leukocyte function-associated antigen-1; luteinizing hormone-releasing hormone; scanning tunneling microscopy; single-molecule force spectroscopy
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Microscopía de Fuerza Atómica
/
Proteínas de la Membrana
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
2014
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Países Bajos