Structural insights into early folding events using continuous-flow time-resolved SAXS
Authors
Kathuria, Sagar V.Guo, Liang
Graceffa, Rita
Barrea, Raul
Nobrega, R. Paul
Matthews, C. Robert
Irving, Tom
Bilsel, Osman
Student Authors
Sagar V. Kathuria; R. Paul NobregaUMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyDocument Type
Journal ArticlePublication Date
2011-03-25Keywords
Scattering, Small Angle; X-Ray Diffraction; Protein Folding; Protein ConformationBiochemistry, Biophysics, and Structural Biology
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
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]DOI
10.1002/bip.21628Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33136PubMed ID
21442608Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1002/bip.21628