Laboratory of Structural Chemistry and Biology Eötvös Loránd University, Institute of Chemistry, Budapest, Hungary

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An EAST-NMR member laboratory The objective of our Laboratory is the structural, dynamical and mechanistic characterization of biological macromolecules using NMR spectropscopy, X-ray crystallography and theoretical methods (quantum chemistry and bioinformatics). We cooperate extensively with a number of other research groups in the field of molecular biology and biochemistry. Head of the lab: Dr. András Perczel, full professor Tel:(36-1) 209-0555 ext. 1653 Fax:(36-1) 372-2620 E-mail: perczel@chem.elte.hu Location: Eötvös Loránd University, Institute of Chemistry Address: Pázmány Péter sétány 1/A, H-1117 Budapest, Hungary From our current research: András László Kiss, Anna Palló, Gábor Náray-Szabó, Veronika Harmat, László Polgár: Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidase. J. Struct. Biol. (2008) 162:312-323. Péter Hudáky, Pál Stráner, Viktor Farkas, Györgyi Váradi, Gábor Tóth, András Perczel: Cooperation between a salt bridge and the hydrophobic core triggers fold stabilization in a Trp-cage miniprotein Biochemistry (2008) 47:1007-1016. Annamária F. Ángyán, András Perczel, Sándor Pongor, Zoltán Gáspári: Fast protein fold estimation from NMR-derived distance restraints Bioinformatics (2008) 24:272-275. András Perczel, Péter Hudáky, Villő K. Pálfi: Dead-End Street of Protein Folding: Thermodynamic Rationale of Amyloid Fibril Formation J. Am. Chem. Soc. (2007) 129:14959 -14965.