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Daus M.L.,FG 14 AG 5 Unconventional Pathogens and Their Inactivation | Beekes M.,FG 14 AG 5 Unconventional Pathogens and Their Inactivation | Lasch P.,Robert Koch Institute
BioSpektrum | Year: 2014

The structure of a protein is of major importance for the understanding of its function. Infrared spectroscopy allows the analysis of protein structure and dynamics, even from large proteins or from proteins with poor crystal-forming properties, without the need of sample labelling or staining. This technique is relatively simple in use and can provide data within a very short time. Therefore, infrared spectroscopy belongs to the methods of choice to study the structure of prions. © 2014 Springer-Verlag Berlin Heidelberg. Literatur:.


Daus M.L.,FG 14 AG 5 Unconventional Pathogens and Their Inactivation | Wagenfuhr K.,FG 14 AG 5 Unconventional Pathogens and Their Inactivation | Thomzig A.,FG 14 AG 5 Unconventional Pathogens and Their Inactivation | Boerner S.,FG 14 AG 5 Unconventional Pathogens and Their Inactivation | And 4 more authors.
Journal of Biological Chemistry | Year: 2013

Background: It is currently under discussion whether protein misfolding cyclic amplification (PMCA) alters strain properties of prions. Results: An improved infrared microspectroscopic approach combined with biochemical and bioassay data revealed altered strain properties of hamster 263K scrapie prions due to PMCA. Conclusion: PMCA can alter strain properties of 263K prions. Significance: Our analytical approach may help to improve the understanding of prion strain conversion. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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