Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering.
Biopolymers
; 95(8): 550-8, 2011 Aug.
Article
en En
| MEDLINE
| ID: mdl-21442608
ABSTRACT
Small-angle X-ray scattering (SAXS) is a powerful method for obtaining quantitative structural information on the size and shape of proteins, and it is increasingly used in kinetic studies of folding and association reactions. In this minireview, we discuss recent developments in using SAXS to obtain structural information on the unfolded ensemble and early folding intermediates of proteins using continuous-flow mixing devices. Interfacing of these micromachined devices to SAXS beamlines has allowed access to the microsecond time regime. The experimental constraints in implementation of turbulence and laminar flow-based mixers with SAXS detection and a comparison of the two approaches are presented. Current improvements and future prospects of microsecond time-resolved SAXS and the synergy with ab initio structure prediction and molecular dynamics simulations are discussed.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Difracción de Rayos X
/
Proteínas
/
Pliegue de Proteína
/
Dispersión del Ángulo Pequeño
Límite:
Animals
Idioma:
En
Revista:
Biopolymers
Año:
2011
Tipo del documento:
Article
País de afiliación:
Estados Unidos