Michal Maj
Biträdande universitetslektor vid Institutionen för kemi - Ångström; Fysikalisk kemi
- E-post:
- michal.maj@kemi.uu.se
- Besöksadress:
- Ångströmlaboratoriet
Lägerhyddsvägen 1
751 20 UPPSALA - Postadress:
- Box 523
751 20 UPPSALA
Ladda ned kontaktuppgifter för Michal Maj vid Institutionen för kemi - Ångström; Fysikalisk kemi
Biträdande universitetslektor vid Institutionen för cell- och molekylärbiologi; Strukturbiologi
- Besöksadress:
- Husargatan 3
752 37 Uppsala - Postadress:
- Box 596
75124 Uppsala
Mer information visas för dig som medarbetare om du loggar in.
Kort presentation
Denna text finns inte på svenska, därför visas den engelska versionen.
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
Publikationer
Senaste publikationer
- 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
Alla publikationer
Artiklar
- 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