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  X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations.

Jain, R., Petri, M., Kirschbaum, S., Feindt, H., Steltenkamp, S., Sonnenkalb, S., et al. (2013). X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations. The European Physical Journal E, 36(9): 109. doi:10.1140/epje/i2013-13109-9.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-7A8F-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CB6E-9
Genre: Journal Article

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 Creators:
Jain, R.1, Author              
Petri, M.1, Author              
Kirschbaum, S.2, Author              
Feindt, H., Author
Steltenkamp, S., Author
Sonnenkalb, S.1, Author              
Becker, S.3, Author              
Griesinger, C.3, Author              
Menzel, A., Author
Burg, T. P.2, Author              
Techert, S.1, Author              
Affiliations:
1Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for biophysical chemistry, Max Planck Society, ou_578564              
2Research Group of Biological Micro- and Nanotechnology, MPI for biophysical chemistry, Max Planck Society, ou_578602              
3Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: Small-angle X-ray scattering provides global, shape-sensitive structural information about macromolecules in solution. Its extension to time dimension in the form of time-resolved SAXS investigations and combination with other time-resolved biophysical methods contributes immensely to the study of protein dynamics. TR-SAXS can also provide unique information about the global structures of transient intermediates during protein dynamics. An experimental set-up with low protein consumption is essential for an extensive use of TR-SAXS experiments on protein dynamics. In this direction, a newly developed 20-microchannel microfluidic continuous-flow mixer was combined with SAXS. With this set-up, we demonstrate ubiquitin unfolding dynamics after rapid mixing with the chaotropic agent Guanidinium-HCl within milliseconds using only 40 nanoliters of the protein sample per scattering image. It is suggested that, in the future, this new TR-SAXS platform will help to increase the use of time-resolved small-angle X-ray scattering, wide-angle X-ray scattering and neutron scattering experiments for studying protein dynamics in the early millisecond regime. The potential research field for this set-up includes protein folding, protein misfolding, aggregation in amyloidogenic diseases, function of intrinsically disordered proteins and various protein-ligand interactions.

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Language(s): eng - English
 Dates: 2013-09-27
 Publication Status: Published online
 Pages: 9
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1140/epje/i2013-13109-9
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Title: The European Physical Journal E
Source Genre: Journal
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Pages: - Volume / Issue: 36 (9) Sequence Number: 109 Start / End Page: - Identifier: -