Expertise

• Numerical modeling
• Computational biophysics
• Molecular dynamics of proteins

Education

• Molecular Dynamics & NMR Group, University of Groningen, NL
• Dep. of Biotechnology, University of Groningen, NL
• St. John's College, Cambridge University, UK

Selected publications

• Sequence-specific random coil chemical shifts of intrinsically disordered proteins. K. Tamiola, B. Acar, F.A.A. Mulder. Journal of the American Chemical Society 132 (51), 18000-18003, (2010)


• Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins. K. Tamiola, F.A.A. Mulder. Biochemical Society Transactions 40 (5), 1014-1020, (2012)


• NMR experimental data to characterize residue specific structural propensity in intrinsically disordered proteins. K. Tamiola, B. Acar, R. Otten, K. Wood, F.A.A. Mulder, (2014)

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Biography

Kamil was born to a family of medical doctors. Inspired by the 1^st edition of Feynman’s lectures on physics, Kamil decided to pursue a purely scientific path, a deed considered as a rebellious act by his parents, given the medical traditions in the family.

The passion for applied physics and computing were instrumental in getting the first peer-reviewed paper accepted, "Seeing and Recognising Objects as Physical Process - Practical and Theoretical Use of Artificial Neural Networks" at the age of 18. The aforementioned article, recognised by the Polish Academy of Sciences, won Kamil an exam-free admission to University of Wroclaw, where he conduced personalised research in the area of computational biophysics with the specialisation in numerical modelling of proteins. Shortly after followed the undergraduate research at Cambridge University with the prestigious Bill Gates foundation scholarship, and the admittance to an elite master degree programme, “Top Master in Bimolecular Sciences”, at University of Groningen, the Netherlands.

Working under the watchful eye of researchers in the Biotechnology Laboratory of Groningen Bimolecular Sciences Institute (GBB), Kamil developed his first industrial-scale numerical models, which have direct implications in the production of an antibiotic: penicillin. His curiosity and passion for high performance computing led him to the laboratory of Molecular Dynamics and Nuclear Magnetic Resonance Spectroscopy (NMR) where he begun his doctoral studies in computational biophysics. Tutored by Prof. Frans A.A. Mulder, Kamil developed highly cited tools and relational database used to characterise a perplexing class of intrinsically disordered proteins (IDPs), directly implicated in neurodegenerative disorders, including “mad cow” disease, and Alzheimer’s.

Expertise

• Protein engineering
• Enzymology
• Enzyme discovery

Education

• Dept. of Biochemistry, University of Groningen, NL
• Institute of Molecular Biology & Biophysics, Swiss Federal Institute of Technology, CH
• Dept. of Biochemistry, The Ohio State University, USA
• Fisher College of Business, The Ohio State University, USA

Selected publications

• Ironing out their differences: Dissecting the structural determinants of a phenylalanine aminomutase and ammonia lyase. M. M. Heberling et al., ACS Chem. Biol. 10, 989–997 (2015)


• Priming ammonia lyases and aminomutases for industrial and therapeutic applications. M. M. Heberling, B. Wu, S. Bartsch, D. B. Janssen, Curr. Opin. Chem. Biol. 17, 250–260 (2013)


• DARPin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein crystallography. A. Batyuk, Y. Wu, A. Honegger, M. M. Heberling, A. Plückthun, J. Mol. Biol. 428 (2016)

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Biography

Matt was born 1978 in small-town, U.S.A. (Ohio). He learned early-on about the power of vision in sports (cross country state), which propelled his career change from tax accountant to protein engineer. His "Ah-ha" moments that sparked this change: reflections on a childhood filled with curiosity and Legos and wondering how scientists study molecules they can't see.

Matt began research with Prof. Tom Magliery (Ohio State U.) after being awarded a scholarship to investigate tumor suppressor protein, p53. Aside from the intellectual growth, Prof. Magliery inspired Matt with effective scientific communication. Intrigued by the intricacies of protein structure-function, his next projects with Prof. Andreas Plueckthun (U. of Zurich) examined innovative approaches for protein structure determination using robust binding proteins. This experience groomed his 'think outside of the box' mentality.

His developed curiosity about proteins that catalyze reactions (enzymes) landed him a doctoral research position with Prof. Dick Janssen (Groningen U.). There, Matt expanded his knowledge into enzyme discovery and engineering, bioinformatics, metagenomics, and microbiology. He focused on the discovery of transaminases and aminomutases for the conversion of unnatural amino acids that led to 6 (co)-authored publications.

Expertise

• Numerical modeling
• Computational biophysics
• Protein folding

Education

• Structural Bioinformatics and Computational Biochemistry Unit, University of Oxford, UK
• Molecular Dynamics Group, University of Groningen, NL
• Merton College, New College, Oxford, UK
• D. E. Shaw Research, NYC

Selected publications

• Lipidbook: a public repository for force-field parameters used in membrane simulations. J Domański, PJ Stansfeld, MSP Sansom, O Beckstein. The Journal of membrane biology 236 (3), 255-258


• Transmembrane helices can induce domain formation in crowded model membranes.J Domański, SJ Marrink, LV Schäfer. Biochimica Et Biophysica Acta (BBA)-Biomembranes 1818 (4), 984-994


• Convergence and Sampling in Determining Free Energy Landscapes for Membrane Protein Association J Domanski, G Hedger, R Best, S PJ, M Sansom. J Phys Chem B

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Biography

Jan obtained his MBioch from Oxford, then started his PhD with NIH/Wellcome Trust funded scholarship working on membrane protein folding. In his spare time, Jan enjoys reading, cycling and spending time with friends.

Expertise

• Computational chemistry
• Biological physics
• Statistical mechanics

Education

• University of Leeds, Leeds, UK
• University of Oxford, Oxford, UK
• Sorbonne Universités, Paris, FR
• Sapienza Università di Roma, Rome, IT

Selected publications

• Effects of Ligand Binding on the Mechanical Properties of Ankyrin Repeat Protein Gankyrin Author(s): Settanni, Giovanni; Serquera, David; Marszalek, Piotr E.; et al. Source: PLoS Computational Biology Volume: 9 Issue: 1 Published: JAN 2013


• Using Models to Design New Bioinspired Materials Author(s): Paci, Emanuele Source: Biophysical Journal Volume: 103 Issue: 9 Pages: 1814-1815 Published: NOV 7 2012


• Direct evidence of the multidimensionality of the free-energy landscapes of proteins revealed by mechanical probes Author(s): Yew, ZT; Schlierf, M; Rief, M; et al. Source: Physical Review E Volume: 81 Issue: 3 Published: 2010

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Most of my research in the past decade has been devoted to advance understanding of properties of macromolecules in biological contexts, by using computer simulations to establish a relation between physical models and experimental measurements. One unique property of biological polymers such as proteins and RNA is their ability to populate a state characterised by a precisely defined conformation, unlike any man-made polymers. Protein folding is one of the major focuses of our recent research, with a particular interest to the relation between folded structure, unfolding pathway and mechanical properties. Our theoretical and computational research in this field has had impact on the way experiments are performed and interpreted, while mechanical response is increasingly recognised as an essential part of many biological processes.

More recently we have turned our interests to the growth of bacterial pili, rational design of symmetric protein complexes such as capsids (with B. Turnbull), analysis of time resolved X-ray spectroscopy data (with A. Pearson), determination of structure and dynamics of macromolecular compounds from cryo-EM (with S. Muench) and hydrogen-exchange mass spectroscopy experiments (with R. Tuma).