Nils Gunnar Hansson von Heijne Professor of Biochemistry
Contact
Name and title: Nils Gunnar Hansson von HeijneProfessor of Biochemistry
ORCID0000-0002-4490-8569 Länk till annan webbplats.
Workplace: Department of Biochemistry and Biophysics Länk till annan webbplats.
Visiting address Room A 435Svante Arrhenius väg 16
Postal address Institutionen för biokemi och biofysik106 91 Stockholm
About me
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, November 2000 – February 2006
Director of the Center for Biomembrane Research, March 2006 – December 2015
Vice Director, Science for Life Laboratory Stockholm, January 2009 – June 2015
Director of the SciLifeLab National Cryo-EM Facility, January 2016 – 2021
Membrane protein assembly and structure.
Membrane proteins serve a number of very important functions in both prokaryotic and eukaryotic cells. They are built according to structural principles different from those of globular proteins. A full understanding of membrane proteins requires a conceptual framework where processes of protein translocation across membranes and the physical chemistry of lipid-protein interactions play major roles.
Work in our lab has pointed to the central importance of positively charged amino acids as determinants of membrane protein topology, has led to the development of new theoretical methods for predicting transmembrane segments, and has illuminated many aspects of membrane protein assembly in both prokaryotic and eukaryotic cells. Ongoing work is directed towards a better understanding of the folding and assembly of membrane proteins.
Cotranslation folding of soluble proteins
We study the cotranslational folding of soluble proteins, mainly using Force Profile Analysis and cryo-EM.
Group members
Ane Metola Martinez, Postdoc
Justin Westerfield, Postdoc
Morgana Kellogg, Postdoc