Investigating how intrinsically disordered regions contribute to protein function using HDX-MS.
Biochem Soc Trans
; 50(6): 1607-1617, 2022 12 16.
Article
en En
| MEDLINE
| ID: mdl-36454645
ABSTRACT
A large amount of the human proteome is composed of highly dynamic regions that do not adopt a single static conformation. These regions are defined as intrinsically disordered, and they are found in a third of all eukaryotic proteins. They play instrumental roles in many aspects of protein signaling, but can be challenging to characterize by biophysical methods. Intriguingly, many of these regions can adopt stable secondary structure upon interaction with a variety of binding partners, including proteins, lipids, and ligands. This review will discuss the application of Hydrogen-deuterium exchange mass spectrometry (HDX-MS) as a powerful biophysical tool that is particularly well suited for structural and functional characterization of intrinsically disordered regions in proteins. A focus will be on the theory of hydrogen exchange, and its practical application to identify disordered regions, as well as characterize how they participate in protein-protein and protein-membrane interfaces. A particular emphasis will be on how HDX-MS data can be presented specifically tailored for analysis of intrinsically disordered regions, as well as the technical aspects that are critical to consider when designing HDX-MS experiments for proteins containing intrinsically disordered regions.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Medición de Intercambio de Deuterio
/
Espectrometría de Masas de Intercambio de Hidrógeno-Deuterio
Límite:
Humans
Idioma:
En
Revista:
Biochem Soc Trans
Año:
2022
Tipo del documento:
Article
País de afiliación:
Canadá