PhD in Theoretical Physics, the Royal Institute of Technology, Stockholm, 1980.
Postdoc, Department of Microbiology and Immunology, University of Michigan, Ann Arbor 1980 – 1981.
Assistant Professor, the Royal Institute of Technology, Stockholm, 1981-1988
Science correspondent for the Swedish National Radio (half-time) 1982 - 1985
Associate Professor, Karolinska Institutet, Stockholm, 1989-1994
Professor of Theoretical Chemistry, Stockholm University, 1994-
Director of Stockholm Bioinformatics Center, 2000 –2006
Director of the Center for Biomembrane Research, 2006 –
Vice Director, Science for Life Laboratory Stockholm, 2009 –
The T. Svedberg Award, The Swedish Biochemical Society, 1990
Elected EMBO member, 1994
The Göran Gustafsson Prize, The Swedish Academy of Sciences, 1995
The Arrhenius Medal, The Swedish Chemical Society, 1997
Elected member of the Royal Swedish Academy of Sciences, 1997
Elected member of the Academia Europaea, 1998
The Björkén Prize, Uppsala University, 1998
Elected member of the Royal Swedish Academy of Engineering Sciences, 2000
Friday Lecturer, Rockefeller University, 2007
Kroc Lecturer, MIT, 2008
Honorary Doctorate, Åbo Akademi, 2008
The van Deenen Medal, Utrecht University, 2009
The Accomplishment by a Senior Scientist Award of the International Society for Computational Biology, 2012.
Member of the Nobel Committee for Chemistry 1998-2009 (Chairman 2007-2009)
Summary of scientific work
Has worked mainly on problems related to protein sorting and membrane protein biogenesis and structure. The work includes both bioinformatics methods development (e.g. methods for prediction of signal peptides and other sorting signals as well as prediction of membrane protein topology) and experimental studies in E. coli and eukaryotic systems.
The most important achievements include the discovery and experimental validation of the so-called “(-1,-3)-rule” (describes signal peptide cleavage sites) and the “positive inside” rule (describes membrane protein topology), the development of widely used prediction methods (e.g., TopPred, SignalP, TargetP, TMHMM), the first proteome-wide theoretical and experimental studies of membrane protein topology in E. coli and S. cerevisiae, the first quantitative analysis of the energetics of membrane protein assembly in vivo, and theoretical and experimental studies of so-called dual-topology membrane proteins and their role in the evolution of membrane protein structure.
Selected publications (out of ~320)
von Heijne, G. (1989) Control of Topology and Mode of Assembly of a Polytopic Membrane Protein by Positively Charged Residues. Nature 341, 456-458.
Gafvelin, G., and von Heijne, G. (1994) Topological “Frustration” in Multi-Spanning E. coli Inner Membrane Proteins. Cell 77, 401-412.
Hessa, T., Kim., H., Bihlmaier, K., Lundin, C., Boekel, J., Andersson, H., Nilsson, I.M., White, S.H., and von Heijne, G. (2005) Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433, 377-381.
Daley, D.O., Rapp, M., Granseth, E., Melén, K., Drew, D., and von Heijne, G. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308, 1321-1323.
Hessa, T., Meindl-Beinker, N.M., Bernsel, A., Kim, H., Sato, Y., Lerch-Bader, M., Nilsson, IM., White, S.H., and von Heijne, G. (2007) Molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature 450, 1026-1030.
Rapp, M., Seppälä, S., Granseth, E., and von Heijne, G. (2007) Emulating membrane protein evolution by rational design. Science 315, 1282-1284.
Seppälä, S., Slusky, J.S., Loris-Garcerá, P., Rapp, M., and von Heijne, G. (2010) Control of membrane protein topology by a single C‑terminal residue. Science 328, 1698-1700.
Öjemalm, K., Halling, K.K., Nilsson, IMN., and von Heijne, G. (2012) Orientational preferences of neighboring helices can drive ER insertion of a marginally hydrophobic transmembrane helix. Mol.Cell 45, 529-540.
Ismail, N., Hedman, R., Schiller, N., and von Heijne, G. (2012) A bi-phasic pulling force acts on transmembrane helices during translocon-mediated membrane integration. Nature Struct. Molec. Biol 19, 1018-1023.