!!Peter Tompa - Biography
Peter Tompa (55) graduated in organic chemistry (1983, ELTE University, Budapest), and obtained his PhD in 1991 (ELTE University, Budapest) based on research carried out in the Institute of Enzymology, Hungarian Academy of Sciences (HAS), Budapest, on the interaction of glycolytic enzymes. He did his postdoc in the same institute under the supervision of Prof. Peter Friedrich on the structure-function characterization of the calcium-activated protease calpain (1992-2001), and became independent PI in 2002. He started research on intrinsically disordered proteins (IDPs) in 2000, and played an active and decisive role in the rise of this field (cf. [http://tompa.enzim.hu]) by suggesting a functional classification of IDPs, observing the role of structural disorder in chaperone function and developing basic concepts of the unusual modes of function of IDPs (moonlighting, fuzziness, disordered domains and the supertertiary structure of proteins). 
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He was the deputy director of the Institute of Enzymology in the period 2007-2009. Currently he is the director of VIB (Flanders Institute of Biotechnology) Department of Structural Biology, Brussels (2011-13), and also a professor at VUB (Free University Brussels, 2012-13). He also holds the position of professor of biochemistry and protein sciences in the Institute of Enzymology, Budapest (2006-2013). He has research groups both in Budapest and Brussels. He published about 138 papers, and the first monograph of the field “Structure and function of intrinsically disordered proteins” (2009) by Taylor and Francis, Inc. (CRC Press). 
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He was an invited speaker at about 90 international conferences, such as the first IDP subgroup meeting at the “51st Annual Meeting of the Biophysical Society” in Baltimore, USA (2007). He organized the first conference of the IDP field, the EMBO workshop “Intrinsically unfolded proteins: from structure to function” in Budapest, Hungary (2007), and chaired the Gordon Research Conference on IDPs in Vest Dover, VT, USA (2012).