Alexander Stevens
PhD student at Department of Cell and Molecular Biology; Molecular Biophysics
- E-mail:
- alexander.stevens@icm.uu.se
- Visiting address:
- Husargatan 3
752 37 Uppsala - Postal address:
- Box 596
751 24 Uppsala
Short presentation
My research is in the field of molecular biophysics, focused on proteins. I'm a part of the lab of Michael Landreh, where we use Native Mass Spectrometry to study how proteins fold, interact, and function. On top of this, I use De Novo protein design to probe methodological parameters and solve problems in certain diseases, primarily concerning disordered proteins.

Publications
Recent publications
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Membrane protein solubilization and structure determination using de novo-designed proteins
Part of Science, 2026
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Part of Analytical Chemistry, p. 10738-10744, 2025
- DOI for Stabilization of Protein Interactions through Electrospray Additives in Negative Ion Mode Native Mass Spectrometry
- Download full text (pdf) of Stabilization of Protein Interactions through Electrospray Additives in Negative Ion Mode Native Mass Spectrometry
-
Part of JACS Au, p. 281-290, 2025
- DOI for Native Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains
- Download full text (pdf) of Native Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains
All publications
Articles in journal
-
Membrane protein solubilization and structure determination using de novo-designed proteins
Part of Science, 2026
-
Part of Analytical Chemistry, p. 10738-10744, 2025
- DOI for Stabilization of Protein Interactions through Electrospray Additives in Negative Ion Mode Native Mass Spectrometry
- Download full text (pdf) of Stabilization of Protein Interactions through Electrospray Additives in Negative Ion Mode Native Mass Spectrometry
-
Part of JACS Au, p. 281-290, 2025
- DOI for Native Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains
- Download full text (pdf) of Native Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains