Gunnar von Heijne | |
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![]() Gunnar von Heijne at ISMB in 2012 | |
Born | Nils Gunnar Hansson von Heijne 10 June 1951 |
Nationality | Swedish |
Awards | Björkénska priset (1998) Accomplishment by a Senior Scientist Award [1] |
Scientific career | |
Fields | Royal Institute of Technology |
Institutions | Stockholm University, Karolinska Institutet |
Professor Nils Gunnar Hansson von Heijne, born 10 June 1951 in Gothenburg, is a Swedish scientist [2] working on signal peptides, membrane proteins [3] [4] [5] and bioinformatics [6] [7] at the Stockholm Center for Biomembrane Research at Stockholm University.
Gunnar von Heijne graduated 1975 with a Master of Science degree in chemistry and chemical engineering from the Royal Institute of Technology (KTH). [8] He then became a doctoral student in theoretical physics at KTH, in a research group focussing on statistical mechanics and theoretical biophysics, and was awarded his Ph.D. in 1980. [9] In 1983 he was made docent in theoretical biophysics at KTH, where he remained until 1988. 1982-1985 he was active as a science reporter at Sveriges Radio. 1989-1994 he was active at Karolinska Institutet, and in 1994 he was made a professor in theoretical chemistry at Stockholm University. [8]
von Heijne's research primarily concerns membrane proteins, and he is one of the most cited Swedish scientists in the areas of biochemistry and molecular biology. [10] He heads the Center for Biomembrane Research at Stockholm University. [11]
In 2012 he was awarded the Accomplishment by a Senior Scientist Award [1] by the International Society for Computational Biology.
von Heijne is a member of the Royal Swedish Academy of Sciences since 1997 and a member of the Nobel Committee for Chemistry from 2001 to 2009, and the Committees chairman from 2007 to 2009. In 2008, he received an honorary doctorate at Åbo Akademi. [10]
Membrane proteins are common proteins that are part of, or interact with, biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane and can either penetrate the membrane (transmembrane) or associate with one or the other side of a membrane. Peripheral membrane proteins are transiently associated with the cell membrane.
Topology of a transmembrane protein refers to locations of N- and C-termini of membrane-spanning polypeptide chain with respect to the inner or outer sides of the biological membrane occupied by the protein.
A signal peptide is a short peptide present at the N-terminus of most newly synthesized proteins that are destined toward the secretory pathway. These proteins include those that reside either inside certain organelles, secreted from the cell, or inserted into most cellular membranes. Although most type I membrane-bound proteins have signal peptides, the majority of type II and multi-spanning membrane-bound proteins are targeted to the secretory pathway by their first transmembrane domain, which biochemically resembles a signal sequence except that it is not cleaved. They are a kind of target peptide.
Søren Brunak is a Danish biological and physical scientist working in bioinformatics, systems biology and medical informatics. He is professor of Disease Systems Biology at the University of Copenhagen and professor of bioinformatics at the Technical University of Denmark. As Research Director at the Novo Nordisk Foundation Center for Protein Research at the University of Copenhagen Medical School he leads a research effort where molecular level systems biology data are combined with phenotypic data from the healthcare sector, such as electronic patient records, registry information and biobank questionnaires. A major aim is to understand the network biology basis for time-ordered comorbidities and discriminate between treatment related disease correlations and other comorbidities in disease trajectories. Søren Brunak also holds a position as Medical Informatics Officer at Rigshospitalet, Capital Region of Denmark.
Carbohydrate kinase domain containing protein, encoded by CARKD gene, is a human protein of unknown function. The CARKD gene encodes proteins with a predicted mitochondrial propeptide (mCARKD), a signal peptide (spCARKD) or neither of them (cCARKD). Confocal microscopy analysis of transfected CHO cells indicated that cCARKD remains in the cytosol, whereas mCARKD and spCARKD are targeted to the mitochondria and the endoplasmic reticulum respectively. The protein is conserved throughout many species, and has predicted orthologs through eukaryotes, bacteria, and archea.
Neuroblastoma breakpoint family, member 15, also known as NBPF15, is a protein which in humans is encoded by the NBPF15 gene. The gene is 18762 bp long, with mRNA that is 3837 bp long. The gene is located on chromosome 1q21.1. Its sub-cellular location is predicted to be in the nucleus and cytoplasm. It contains what is known as the NBPF repeat, which is a two-exon stretch of sequence that is characteristic of all 21 members of the NBPF gene family. The repeat is considered the ancestral exons, and the NBPF family has been linked to primate evolution.
Transmembrane protein 126B is a protein that in humans is encoded by the TMEM126B gene. TMEM126B is a mitochondrial transmembrane protein which is a component of the mitochondrial complex I assembly complex. The TMEM126B gene is conserved in mammals. The encoded protein serves as an assembly factor that is required for formation of the membrane arm of the complex. It interacts with NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 13. Naturally occurring mutations in this gene are associated with isolated complex I deficiency. A pseudogene of this gene has been defined on chromosome 9.
KIAA0090 is a human gene coding for a protein of unknown function. KIAA0090 has two aliases OTTHUMP00000002581 and RP1-43E13.1. The gene codes for multiple transcript variants which can localize to different subcellular compartments. KIAA0090 interacts with multiple effector proteins. KIAA0090 contains a conserved COG1520 WD40 like repeat domain thought to be the method of such interaction.
The ISCB Accomplishment by a Senior Scientist Award is an annual prize awarded by the International Society for Computational Biology for contributions to the field of computational biology.
QRICH1, also known as Glutamine-rich protein 1, is a protein that in humans is encoded by the QRICH1 gene. One notable feature of this protein is that it contains a Caspase Activation Recruitment Domain, also known as a CARD domain. As a result of having this domain, QRICH1 is believed to be involved in apoptotic, inflammatory, and host-immune response pathways.
TMEM106A is a gene that encodes the transmembrane protein 106A (TMEM106A) in Homo sapiens. It is located at 17q21.31 on the plus strand next to cancer-related genes NBR1 and BRCA1. The TMEM106A gene contains a domain of unknown function, DUF1356.
Protein FAM83A also known as tumor antigen BJ-TSA-9 is a protein that in humans is encoded by the FAM83A gene.
Alfonso Valencia is a Spanish biologist, ICREA Professor, current director of the Life Sciences department at Barcelona Supercomputing Center. and of Spanish National Bioinformatics Institute (INB-ISCIII). From 2015-2018, he was President of the International Society for Computational Biology. His research is focused on the study of biomedical systems with computational biology and bioinformatics approaches.
CXorf66 also known as Chromosome X Open Reading Frame 66, is a 361aa protein in humans that is encoded by the CXorf66 gene. The protein encoded is predicted to be a type 1 transmembrane protein; however, its exact function is currently unknown. CXorf66 has one alias: RP11-35F15.2.
Stephen H. White is an American Biophysicist, academic, and author. He is a Professor Emeritus of Physiology and Biophysics at the University of California, Irvine.
Leucine-Rich Single-Pass Membrane Protein 1 (LSMEM1) is a protein that, in humans, is encoded by the LSMEM1 gene.
Leucine rich repeat containing 24 is a protein that, in humans, is encoded by the LRRC24 gene. The protein is represented by the official symbol LRRC24, and is alternatively known as LRRC14OS. The function of LRRC24 is currently unknown. It is a member of the leucine-rich repeat (LRR) superfamily of proteins.
Hanah Margalit is a Professor in the faculty of medicine at the Hebrew University of Jerusalem. Her research combines bioinformatics, computational biology and systems biology, specifically in the fields of gene regulation in bacteria and eukaryotes.
Shuguang Zhang is an American biochemist. He is at the MIT Media Lab's Laboratory for Molecular Architecture. Shuguang Zhang's research focuses on designs of biological molecules, particularly proteins and peptides. He has published over 170 scientific papers, which have cumulatively been cited over 35,000 times with an h-index of 88. On the “Updated science-wide author databases of standardizes citation indicators”, he is ranked 18th worldwide in the field of Biomedical Engineering. Zhang is also a co-founder and board member of Molecular Frontiers Foundation, which organizes annual Molecular Frontiers Symposia in Sweden and around the world. The selected winners are awarded Molecular Frontiers Inquiry Prize.