Nenad Ban | |
---|---|
Born | Zagreb, Croatia | May 3, 1966
Nationality | Croatian |
Alma mater | University of Zagreb, Croatia, University of California at Riverside |
Known for | Structural biology, structure and function of the ribosome, structure and function of multi-enzymes |
Spouse | Eilika Weber-Ban |
Awards | Newcomb Cleveland Prize (2001) Rössler Prize (2009) Heinrich Wieland Prize (2010) Ernst Jung Prize (2017) Otto Naegeli Prize (2018) |
Scientific career | |
Fields | Biochemistry and Biophysics |
Institutions | ETH Zurich |
Doctoral advisor | Alexander McPherson |
Other academic advisors | Thomas A. Steitz |
Nenad Ban is a biochemist born in Zagreb, Croatia who currently works at the ETH Zurich, Swiss Federal Institute of Technology, as a professor of Structural Molecular Biology. He is a pioneer in studying gene expression mechanisms and the participating protein synthesis machinery.
Nenad Ban was born in 1966 in Zagreb. His parents, Jasna and Zvonimir, were scientists and university professors. [1] He received a degree in molecular biology at the Faculty of Science, University of Zagreb and decided to continue with his studies in the United States where he obtained a PhD degree at the University of California, Riverside in the laboratory of Alexander McPherson. He carried out his postdoctoral studies at Yale University in the laboratory of Thomas A. Steitz.
Already in high school he developed an interest in understanding the mechanisms of protein synthesis, which led him to the laboratory of Prof. Zeljko Kucan and Ivana Weygand in Zagreb where he investigated tRNA synthetases, enzymes that charge tRNAs with amino acids to prepare them as substrates for protein synthesis on the ribosome. These interests brought him to the Department of Molecular Biophysics and Biochemistry at Yale University where he determined the atomic structure of the large ribosomal subunit by X-ray crystallography, as part of the group in the laboratory of Thomas A. Steitz. These results demonstrated that the ribosome is a ribozyme. [2]
Since 2000 Nenad Ban is a professor of structural molecular biology at the ETH Zurich. [3] (Swiss Federal Institute of Technology). His group is investigating protein synthesis both in terms of the chemistry of the process and with respect to how it is regulated, how proteins co-translationally fold, [4] [5] how they are co-translationally modified, [6] and how they are targeted to membranes [7] and sorted to different cellular compartments. [8] [9] [10] [11]
Nenad Ban’s group at ETH Zurich revealed the mechanisms behind the key steps in eukaryotic cytoplasmic and mitochondrial translation with a broad impact on a wide range of fields in biology, chemistry and biomedicine. [12] [13]
His group also contributed to our understanding of giant multifunctional enzymes involved in fatty acid synthesis offering mechanistic insights into substrate shuttling and delivery in such megasynthases. [14] [15] [16] [17] [18]
Nenad Ban is a member of the National Academy of Sciences, the European Molecular Biology Organization (EMBO), the German Academy of Sciences, the Croatian Academy of Arts and Sciences and the recipient of several prizes and awards including the Heinrich Wieland Prize, [19] Rössler Prize of the ETH Zurich, [20] the Latsis prize, [21] the Friedrich Miescher Prize of the Swiss Society for Biochemistry, [22] Spiridon Brusina medal, the AAAS Newcomb Cleveland Prize. [23] and the Jung Prize. [24]
Ban is married to Eilika Weber, a German scientist whom he met in the United States during his doctoral study. They have two sons, Arvid and Ivo. [1]
Ribosomes are macromolecular machines, found within all cells, that perform biological protein synthesis. Ribosomes link amino acids together in the order specified by the codons of messenger RNA (mRNA) molecules to form polypeptide chains. Ribosomes consist of two major components: the small and large ribosomal subunits. Each subunit consists of one or more ribosomal RNA (rRNA) molecules and many ribosomal proteins. The ribosomes and associated molecules are also known as the translational apparatus.
Rudolf Grimm is an experimental physicist from Austria. His work centres on ultracold atoms and quantum gases. He was the first scientist worldwide who, with his team, succeeded in realizing a Bose–Einstein condensation of molecules.
Venkatraman "Venki" Ramakrishnan is an Indian-born British and American structural biologist. He shared the 2009 Nobel Prize in Chemistry with Thomas A. Steitz and Ada Yonath for research on the structure and function of ribosomes.
Lumazine synthase (EC 2.5.1.78, 6,7-dimethyl-8-ribityllumazine synthase, 6,7-dimethyl-8-ribityllumazine synthase 2, 6,7-dimethyl-8-ribityllumazine synthase 1, lumazine synthase 2, lumazine synthase 1, type I lumazine synthase, type II lumazine synthase, RIB4, MJ0303, RibH, Pbls, MbtLS, RibH1 protein, RibH2 protein, RibH1, RibH2) is an enzyme with systematic name 5-amino-6-(D-ribitylamino)uracil butanedionetransferase. This enzyme catalyses the following chemical reaction
Leukotriene A4(LTA4) is a leukotriene, and is the precursor for the productions of LTB4 (leukotriene B)) and LTC4 (leukotriene C4).
The 5S ribosomal RNA is an approximately 120 nucleotide-long ribosomal RNA molecule with a mass of 40 kDa. It is a structural and functional component of the large subunit of the ribosome in all domains of life, with the exception of mitochondrial ribosomes of fungi and animals. The designation 5S refers to the molecule's sedimentation velocity in an ultracentrifuge, which is measured in Svedberg units (S).
William (Bill) DeGrado is a professor at the University of California, San Francisco, where he is the Toby Herfindal Presidential Professor of Entrepreneurship and Innovation in the Department of Pharmaceutical Chemistry. As an early pioneer of protein design, he coined the term de novo protein design. He is also active in discovery of small molecule drugs for a variety of human diseases. He is a member of the U.S. National Academy of Sciences (1999), American Academy of Arts & Sciences (1997) and National Academy of Inventors. He also is a scientific cofounder of Pliant therapeutics.
50S is the larger subunit of the 70S ribosome of prokaryotes, i.e. bacteria and archaea. It is the site of inhibition for antibiotics such as macrolides, chloramphenicol, clindamycin, and the pleuromutilins. It includes the 5S ribosomal RNA and 23S ribosomal RNA.
Ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. The 60S subunit is the large subunit of eukaryotic 80S ribosomes. It is structurally and functionally related to the 50S subunit of 70S prokaryotic ribosomes. However, the 60S subunit is much larger than the prokaryotic 50S subunit and contains many additional protein segments, as well as ribosomal RNA expansion segments.
Fatty-acyl-CoA Synthase, or more commonly known as yeast fatty acid synthase, is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.
The eukaryotic small ribosomal subunit (40S) is the smaller subunit of the eukaryotic 80S ribosomes, with the other major component being the large ribosomal subunit (60S). The "40S" and "60S" names originate from the convention that ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. It is structurally and functionally related to the 30S subunit of 70S prokaryotic ribosomes. However, the 40S subunit is much larger than the prokaryotic 30S subunit and contains many additional protein segments, as well as rRNA expansion segments.
Simple Sequence Length Polymorphisms (SSLPs) are used as genetic markers with polymerase chain reaction (PCR). An SSLP is a type of polymorphism: a difference in DNA sequence amongst individuals. SSLPs are repeated sequences over varying base lengths in intergenic regions of deoxyribonucleic acid (DNA). Variance in the length of SSLPs can be used to understand genetic variation between two individuals in a certain species.
Ribosomes are a large and complex molecular machine that catalyzes the synthesis of proteins, referred to as translation. The ribosome selects aminoacylated transfer RNAs (tRNAs) based on the sequence of a protein-encoding messenger RNA (mRNA) and covalently links the amino acids into a polypeptide chain. Ribosomes from all organisms share a highly conserved catalytic center. However, the ribosomes of eukaryotes are much larger than prokaryotic ribosomes and subject to more complex regulation and biogenesis pathways. Eukaryotic ribosomes are also known as 80S ribosomes, referring to their sedimentation coefficients in Svedberg units, because they sediment faster than the prokaryotic (70S) ribosomes. Eukaryotic ribosomes have two unequal subunits, designated small subunit (40S) and large subunit (60S) according to their sedimentation coefficients. Both subunits contain dozens of ribosomal proteins arranged on a scaffold composed of ribosomal RNA (rRNA). The small subunit monitors the complementarity between tRNA anticodon and mRNA, while the large subunit catalyzes peptide bond formation.
Nucleic acid tertiary structure is the three-dimensional shape of a nucleic acid polymer. RNA and DNA molecules are capable of diverse functions ranging from molecular recognition to catalysis. Such functions require a precise three-dimensional structure. While such structures are diverse and seemingly complex, they are composed of recurring, easily recognizable tertiary structural motifs that serve as molecular building blocks. Some of the most common motifs for RNA and DNA tertiary structure are described below, but this information is based on a limited number of solved structures. Many more tertiary structural motifs will be revealed as new RNA and DNA molecules are structurally characterized.
Philippe Guyot-Sionnest is a professor at the University of Chicago appointed jointly in the departments of physics and chemistry. He works in the field of colloidal semiconductors and metal nanocrystals.
Johannes Buchner is a German biochemist and professor at the Technische Universität München, Munich, Germany.
Jochen Mannhart is a German physicist.
The mitochondrial ribosome, or mitoribosome, is a protein complex that is active in mitochondria and functions as a riboprotein for translating mitochondrial mRNAs encoded in mtDNA. The mitoribosome is attached to the inner mitochondrial membrane. Mitoribosomes, like cytoplasmic ribosomes, consist of two subunits — large (mt-LSU) and small (mt-SSU). Mitoribosomes consist of several specific proteins and fewer rRNAs. While mitochondrial rRNAs are encoded in the mitochondrial genome, the proteins that make up mitoribosomes are encoded in the nucleus and assembled by cytoplasmic ribosomes before being implanted into the mitochondria.
Andrew P. Carter is a British structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He is known for his work on the microtubule motor dynein.
Philipp Holliger is a Swiss molecular biologist best known for his work on xeno nucleic acids (XNAs) and RNA engineering. Holliger is a program leader at the MRC Laboratory of Molecular Biology.