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09.45 Key lecture: Vladimir Uversky: Did you mis- it or non-? Protein folding, 10.25 Pierre Goloubinoff - University of Lausanne, Switzerland: Oxana V. Galzitskaya - Institute of Protein Research, Russia: How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation? Experimental application for insulin and LysPro insulin 11.30 Claudio M. Gomes, Universidade Nova de Lisboa, Portugal: Small molecules at the rescue of misfolded proteins Alberto Barbiroli, University of Milan, Italy: Dissecting the stabilizing effects of polyols on protein structure Rajiv Bhat, Jawaharlal Nehru University, India: Understanding solvent-mediated protein stability effects: spectroscopic and calorimetric studies on glucose oxidase in the presence of polyols Jianxing Song, National University of Singapore, Singapore: Why are Aggregated Proteins Toxic? Secrets of “Insoluble Proteins” Eduardo P. Melo, University of Algarve, Portugal:Osmolytes induce compaction of the protein tertiary structure preventing amyloid fiber formation and protein aggregation below the freezing temperature 15.00 Liel Sapir - The Hebrew University of Jerusalem, Israel: How osmolytes induce enthalpic protein stabilization Marina Rubini - University of Konstanz, Germany: (4R)- and (4S)- Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering Josè Luis Vázquez-Ibar - Autonomous University of Barcelona: A general strategy to build stability in a membrane transport protein for Pannuru Venkatesu, University of Delhi, India: Ammonium ionic liquids as biocompatible co-solvents for the structure and stability of proteins 16.50 Reinhard Boysen, Monash University, Australia: Effects of salt types on protein shape determined by small angle X-ray scattering Paul Dalby, University College London, UK: Rapid measurement of protein stability in nanolitre samples using optically induced thermal Andreas Zimmer, University of Graz, Austria: Thermostability of protein formulations: Screening in combination with design of Ulrich Roessl, Graz University of Technology, Austria: Probing conformational stability of pharmaceutical proteins in the frozen state Anna Oom, Biolin Scientific, Sweden: QCM-D in protein drug formulation and storage 18.50 Welcome Cocktail @ poster session 3. Methods to improve stability and solubility: Protein engineering 09.00 Key lecture: Donald Hilvert, ETH, Zurich, Switzerland: Directed evolution of intrinsically disordered enzymes Vladimir I. Tishkov, Lomonosov Moscow State University, Russia: Engineering stability and catalytic properties of D-amino acid oxidase Ayelet Fishman, Technion, Haifa, Israel: Different means of stabilizing enzymes in organic solvents – a tale of two enzymes Javier Sancho, University of Zaragoza, Spain: The divide and combine approach for protein thermostabilization Anastasia Alekseeva, Lomonosov Moscow State University, Russia: Synergetic effect of several single point mutations on stability and kinetic properties of plant formate dehydrogenase 4. Methods to improve stability and solubility: media and supports Key lecture: Karl-Erich Jaeger, Düsseldorf, Germany: CATIBs – highly stable, catalytically-active enzyme inclusion bodies Rafael Vazquez-Duhalt, Universidad Nacional Autonoma de Mexico, Mexico:Virus-like nanoparticles As potential carriers of cytochrome P450 for chemotherapy pro-drug activation Carmen Boeriu, Biobased Products, The Netherlands: Increasing operational stability of oleate hydratase by immobilization Tamo Fukamizo, Kinki University, Japan: Unusual stabilization effects of oligosaccharide binding on chitosan-binding proteins 15.30 Imre Hegedus - University of Pannonia, Hungary: Enzyme stabilization as single enzyme nanoparticles for hydrolysis of Christophe Tribet - Ecole Normale Superieure, France: Toward artificial photo-chaperons: unfolding of model enzymes upon interaction with light-responsive polymers in water Ipsita Roy - Natl Institute of Pharmaceutical Education and Res., India: Nucleic acid aptamers as potential ‘universal’ stabilizers of proteins Christopher Schoene - University of Oxford, UK: SpyTag/SpyCatcher ligation confers resistance to boiling to a mesophilic enzyme 17.20 Giuseppe Bellavia - Université Lille, France: Role of glycerol on trehalose to enhance biostability in relation with fast anharmonic and quasi-harmonic motion Valentina Aina - University of Torino, Italy: Novel smart bio-nanomaterials for protein immobilization: bioactive glasses containing metal nanoparticles conjugated with proteins 09.00 Key lecture: Paolo Carloni - Forschungszentrum Jülich, Germany: Investigating the stability of proteins against aggregation by simulation Vytas Švedas - Lomonosov Moscow State University, Russia: Computational design of stabilized penicillin acylase to improve its catalytic performance in alkaline medium George Makhatadze - Rensselaer Polytechnic Institute, USA: Effect of ionizable residues on the folding energy landscape of globular proteins: linking experiment and computation. Koen Beerens - Masaryk University, Czech Republic: Reliable in silico design of highly stable multiple-point mutants of haloalkane dehalogenase Juergen Pleiss - University of Stuttgart, Germany: Simulation of activity and stability of C.antarctica lipase B under non-natural conditions 6. Stability towards industrial applications 11.30 Key lecture: Massimo Morbidelli, ETH, Zurich, Switzerland Role of Aggregation in the Manufacturing and Formulation of Jan Jezek - Arecor, Cambridge, UK: Innovative approaches to Alessandra Basso - Purolite, South Wales UK: Designing immobilized transaminases for fast screening for hits in the development of new pharmaceutical molecules 15.00 Frank Hollmann - TU Delft, The Netherlands: On the mutual inactivation of transition metals and enzymes Marc Vanhove, Thrombogenics N.V., Belgium: Inactivation of ocriplasmin in eye vitreous: a complex mechanism unraveled by Sebastiana Angelaccio, University of Roma, Italy: Cofactor binding as protein stability determinant in psychrophilic SHMT Willem J.J. van Berkel, Wageningen University, The Netherlands: Bifunctional immobilization of a hyperthermostable endo ß 1,3 Mariam M. Nuhu, University of Manchester, UK: Effect of dipeptides as novel formulation excipients in insulin aggregation and stabilization Christopher Sayer, University of Exeter, UK: Thermostable Enzymes for Industrial Biocatalysis


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Ending Your Pregnancy What is abortion? Abortion means ending a pregnancy. Most abortions are done in the firsttrimester (the first 3 months of the pregnancy). They are done by a doctorand other health care professionals in a hospital, doctor’s office or healthcenter. There are 2 types of abortion: medical and surgical. What is medical abortion? It is an abortion caused by medicine.

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