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 storage18.50 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
Summary of prescribing guidance for thetreatment and prophylaxis of influenza-likeillness: TREATMENT PHASEThis guidance is intended to enable health protection units (HPUs) to address local queries aboutthe treatment and prophylaxis of influenza A(H1N1). It is not a substitute for the Summary ofProduct Characteristics (SPC) and the Patient Information Leaflet (PIL) which must accompany theFurt
ESTATUTOS SECÇÃO I DENOMINAÇÃO E NATUREZA A Associação Rural de Ajuda Social e Jurídica à Criança Moçambicana, ora em diante designada por ARASOCRIMO, é uma pessoa colectiva de Direito Privado, dotado de personalidade jurídica, autonomia financeira, administrativa e patrimonial, sem fins lucrativos, constituída nos termos da lei, regendo-se pelos presentes estatutos e dem