Caroline Jegerschöld CV
Many biochemical reactions occur only after formation of protein complexes in or on the cell membranes. The overall focus in my research is how structure can be related to function of membrane proteins and complexes thereof. Both so called electron crystallography for atomic resolution structures of trans-membrane proteins as well as ‘single particle’ techniques for complex formation between proteins in/on nanodiscs are used in these studies. We have focused to some extent on proteins in the inflammatory prostaglandin and leukotriene biosynthesis pathways but are also working on several other proteins of human or bacterial origin.
For high resolution structures the close view of an active site gives an understanding how substrates or drugs bind and act. For complexes the structure could hint to other locations on the proteins to target than the active site. A membrane protein inserted into a nanodisc has thereby become soluble and could potentially be used as a biological drug. As many drug candidates are strongly hydrophobic nanodiscs (or HDL its native origin) could be used for drug delivery instead of liposomes. Visualization on a molecular level may be essential for the success of drug development.
Ph.D in Biochemistry, Stockholm University, 1996
M.Sci. in Biochemical Technology, Royal Institute of Technology, 1988
Responsible for HL2025 Structural biology and Cell biology, master course at STH/KTH. Supervisor for both doctoral and master students.