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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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Jain, R.1, Autor           
Petri, M.1, Autor           
Kirschbaum, S.2, Autor           
Feindt, H., Autor
Steltenkamp, S., Autor
Sonnenkalb, S.1, Autor           
Becker, S.3, Autor           
Griesinger, C.3, Autor           
Menzel, A., Autor
Burg, T. P.2, Autor           
Techert, S.1, Autor           
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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 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2013-09-27
 Publikationsstatus: Online veröffentlicht
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1140/epje/i2013-13109-9
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Titel: The European Physical Journal E
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 36 (9) Artikelnummer: 109 Start- / Endseite: - Identifikator: -