Zsófia Sólyom


Having developed a deep interest in biochemistry and physics during her high school education, Zsófia participated in a research project concerning the sensitivity of NMR in drug quality control at Gedeon Richter pharmaceutical company yielding her the grand prize of the Hungarian National Pupils' Research Conference. Zsófia graduated in chemical engineering at the Budapest University of Technology and Economics with a bachelor thesis about a quantum chemical study on the stabilization of phosphinidenes and a master thesis about a theoretical study on the hydrolysis of phosphorus trichloride. During her studies she acquired practical skills in the field of proteomics by doing an internship at the Molecular Biology Laboratories of Hoffmann-La Roche. She spent one academic year of her studies at the Joseph Fourier University in Grenoble where she completed the three-month research project "NMR investigation of conformational dynamics in a highly disordered HCV protein" at the Institute of Structural Biology. She has been appointed by CNRS-IBS group within the IDPbyNMR project.



Zsófia Sólyom
Project Topic
NMR characterization of the 257 residues intrinsically disordered fragment of NS5A protein of hepatitis C virus
Project Description
The project aims at developing and optimizing multidimensional fast liquid-state NMR methods for the characterization of structure, dynamics and interactions of intrinsically disordered proteins (IDPs), using longitudal relaxation optimization techniques. The biologically relevant molecular system chosen for application is Non-structural 5A protein (NS5A) of hepatitis C virus (HCV). NS5A plays a key role in the replication of HCV, thus it is a promising drug target. The 447 residues phosphoprotein consists of an amphipatic helix, a structured domain (D1) containing a zinc-binding site, followed by a C-terminal part of about 260 residues (domains 2 and 3) that has been characterized as belonging to the IDP class. The C-terminal domains 2 and 3 also contain various binding motifs that interact with a variety of other viral and human proteins. In particular the interaction of the polyproline motif in the intrinsically disordered domain 2 of NS5A is studied with the SH3 domain of the tumor suppressor host protein Bin1. 

Project Home
Supervisor Bernhard Brutscher

Starting Date
September 2011


Gil, Sergio, Tomáš Hošek, Zsofia Solyom, Rainer Kümmerle, Bernhard Brutscher, Roberta Pierattelli, and Isabella C Felli. 
“NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.” 
Angewandte Chemie 52(45): 11808–12. (2013)

Sophie Feuerstein, Zsofia Solyom, Amine Aladag, Adrien Favier, Melanie Schwarten, Silke Hoffmann, Dieter Willbold, and Bernhard Brutscher.
Transient Structure and SH3 Interaction Sites in an Intrinsically Disordered Fragment of the Hepatitis C Virus Protein NS5A.
J. Mol. Biol., vol. 420 (4-5) pp. 310-323 (2012)

Sophie Feuerstein, Zsofia Solyom, Amine Aladag, Silke Hoffmann, Dieter Willbold, and Bernhard Brutscher.
1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A.
Biomol NMR Assign, vol. 5 (2) pp. 241-243 (2011)


Intensive Training Module – Marie Curie Training Network
Protein Structure Analysis using NMR Chemical Shifts
May 2012 - Cambridge, United Kingdom

Complementary Skills Training – Marie Curie Training Network
Self Marketing, Project Management, Benchmarks and Competition in Research
February 2012 - St. Moritz, Switzerland

Intensive Training Course – Marie Curie Training Network
Bioinformatics and Structural biology of IDPs
October 2011 - Budapest, Hungary