GSBS Student Publications


Structural insights into early folding events using continuous-flow time-resolved SAXS

Student Author(s)

Sagar V. Kathuria; R. Paul Nobrega

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology



Document Type


Medical Subject Headings

Scattering, Small Angle; X-Ray Diffraction; Protein Folding; Protein Conformation


Biochemistry, Biophysics, and Structural Biology | Life Sciences | Medicine and Health Sciences


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 mini-review, 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. © 2011 Wiley Periodicals, Inc. Biopolymers, 2011.

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Citation: Kathuria, S. V., Guo, L., Graceffa, R., Barrea, R., Nobrega, R. P., Matthews, C. R., Irving, T. and Bilsel, O. (2011), Structural insights into early folding events using continuous-flow time-resolved SAXS. Biopolymers, 95: n/a. doi: 10.1002/bip.21628. [Epub ahead of print]

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Link to article in PubMed

PubMed ID