Prof Gunnar von Heijne
Person photo
Organisation: Department of Biochemistry and Biophysics
Phone: +46 8 16 2590
Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16C SE-106 91 Stockholm Sweden


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.

Contracts (16)
Collaborating with (23)
A European Network for Integrated Genome Annotation
Period: 1/1/04 - 12/31/08
The objective of the BIOSAPIENS Network of Excellence is to provide an infrastructure to support a large scale, concerted effort to annotate genome data by laboratories distributed around Europe. This will use both informatics tools and input from experimentalists. Experimental validation of a ...
A systems approach to defining membrane protein networks and applications
Period: 9/1/08 - 8/31/12
Membrane proteins are macromolecules of huge academic and biotechnological importance. They account for ~30% of genes in prokaryotic and eukaryotic genomes, and perform a spectrum of essential cellular functions. Despite their importance, these proteins are poorly understood with respect to ...
Biogenesis of prokaryotic membrane proteins
Period: 1/1/11 - 12/31/14
The project has five main aims: (i) to measure the free energy of insertion of model transmembrane segments into the inner membrane of E. coli; (ii) to measure the force exerted on model transmembrane segments during insertion into the inner membrane of E. coli; (iii) to study the mechanism of ...
Period: 6/1/99 - 12/31/06
Chemical biology studies of protein-lipid interactions
Period: 8/1/09 - 8/31/12
The project aims to combine (i) an in vitro transcription/translation system, developed by the Swedish partner, that makes it possible to measure the free energy of interaction between amino acids incorporated into a transmembrane alpha-helix and the endoplasmic reticulum membrane, with (ii) the ...
Co-translational folding of water-soluble and membrane proteins
Period: 1/1/15 - 12/31/19
Ungefär 30% av alla proteiner som uttrycks i en cell är membranproteiner. Trots membranproteinernas stora betydelse, både inom den grundläggande biologin och för läkemedelsutveckling, saknas fortfarande viktig kunskap om hur de tillverkas, sätts in i ett membran och veckar sig till en aktiv ...
Membrane protein structure prediction based on ROSETTA
Period: 11/1/06 - 4/30/10
Integral helical membrane proteins constitute about 20% of all proteins encoded by most genomes and they play crucial role in cell function and communication. In addition, the medical importance of membrane bound receptors, channels, and pumps as targets f or drugs are well established. However, ...