Structural insights into early folding events using continuous-flow time-resolved SAXS
Biochemistry & Molecular Pharmacology
Department of Biochemistry and Molecular Pharmacology
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.
DOI of Published Version
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]
Kathuria SV, Guo L, Graceffa R, Barrea R, Nobrega RP, Matthews CR, Irving T, Bilsel O. (2011). Structural insights into early folding events using continuous-flow time-resolved SAXS. GSBS Student Publications. https://doi.org/10.1002/bip.21628. Retrieved from https://escholarship.umassmed.edu/gsbs_sp/1678