title: Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering.
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.
authors: Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
authors: Sagar V
authors: SV
authors: Kathuria
authors: Liang
authors: L
authors: Guo
authors: Rita
authors: R
authors: Graceffa
authors: Raul
authors: R
authors: Barrea
authors: R Paul
authors: RP
authors: Nobrega
authors: C Robert
authors: CR
authors: Matthews
authors: Thomas C
authors: TC
authors: Irving
authors: Osman
authors: O
authors: Bilsel
mesh_terms: D000818:Animals; D009682:Magnetic Resonance Spectroscopy; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D053838:Scattering, Small Angle; D012996:Solutions / Q000737:chemistry; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D011506:Proteins; D012996:Solutions