Michal Maj
Associate senior lecturer/Assistant Professor at Department of Chemistry - Ångström Laboratory; Physical Chemistry
- E-mail:
- michal.maj@kemi.uu.se
- Visiting address:
- Ångströmlaboratoriet
Lägerhyddsvägen 1
751 20 UPPSALA - Postal address:
- Box 523
751 20 UPPSALA
Associate senior lecturer/Assistant Professor at Department of Cell and Molecular Biology; Structural Biology
- Visiting address:
- Husargatan 3
752 37 Uppsala - Postal address:
- Box 596
75124 Uppsala
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Short presentation
Research in the Maj group focuses on studying the structure and aggregation kinetics of toxic amyloid intermediates using femtosecond two-dimensional infrared (2D-IR) spectroscopy and cryo-electron microscopy. To increase the structural specificity of 2D-IR, we develop new molecular probes that can be used as IR-active sensors of site-specific structure and dynamics of biomolecules.
For more information see https://www.majgroup.net
Publications
Recent publications
- Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography (2024)
- Improving cryo-EM grids for amyloid fibrils using interface-active solutions and spectator proteins (2024)
- Protein cohabitation (2023)
- Ground-state heterogeneity and vibrational energy redistribution in bacterial phytochrome observed with femtosecond 2D IR spectroscopy (2023)
- Directed ultrafast conformational changes accompany electrontransfer in a photolyase as resolved by serial crystallography
All publications
Articles
- Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography (2024)
- Improving cryo-EM grids for amyloid fibrils using interface-active solutions and spectator proteins (2024)
- Protein cohabitation (2023)
- Ground-state heterogeneity and vibrational energy redistribution in bacterial phytochrome observed with femtosecond 2D IR spectroscopy (2023)
- Directed ultrafast conformational changes accompany electrontransfer in a photolyase as resolved by serial crystallography
