Welcome to BioComp group

The BioComp group at Universitat Jaume I leaded by Prof. Vicent Moliner is devoted to the computational description of catalysis phenomena in biological systems, mostly enzyme catalyzed processes. For this purpose, theories, methods and techniques of theoretical and computational chemistry are developed, implemented and used. Computational algorithms and protocols, based on hybrid QM/MM potentials, are created and this new knowledge is exploited in designing new materials with properties to be used in biomedicine and biotechnology. In particular, these applications are focused on elucidating enzyme reaction mechanisms including fundamental new quantum and dynamical perspectives, to design new pharmacological agents to inhibit enzyme activity, or new catalysts mimicking the catalytic efficiency and features of natural enzymes.

Go to BioComp DeProtCa project >>

LATEST PUBLICATIONS:

E. Gabirondo, A. Maiz-Iginitz, M. Ximenis, K. Świderek, D. Andrés-Sanz, V. Moliner, L. Cabedo, A. H. Westlie, E. Y.-X. Chen, D. Alonso Cerrón-Infantes, M. M. Unterlass, F. López Gallego, A. Etxeberria, H. Sardon "Selective chemical recycling of polyhydroxybutyrate into high-value hydroxy acid using Taurine organocatalyst" Chem. Sci. 16, 2025 DOI:10.1039/D5SC02196K

M. Bemelmans, B. Wetzel, F. Neusius, F. Tieves, C. Schwarz, I. Mateljak, K. Świderek, V. Moliner, M. Alcalde, V. Sieber "Engineering the Tobacco Etch Virus protease towards a platform for traceless cleavage using distal site prediction and smart library design" ACS Synth. Biol.  14, 3721–3733 (2025) DOI: 10.1021/acssynbio.5c00423

S.F. Castillo Pacheco, K. Świderek, M. J. Moran, A. Oliden-Sánchez, V. Moliner, L. Salassa, F. López-Gallego "Overcoming Flavin-Driven Inactivation of Alcohol Dehydrogenases Through Enzyme Immobilization" Catal. Sci. Technol., 2025 DOI:10.26434/chemrxiv-2025-hws7g

H. S. da Costa, C. A. B. de Freitas, A. M. Dos Santos, C. G. da S. de Souza, J. R. A. Silva, J. Lameira, V. Moliner, M. S. Skaf  "Conformational Dynamics and Binding Interactions of SARS-CoV-2 Spike Protein Variants: Omicron, XBB.1.9.2, and EG.5" J. Chem. Inf. Model. 65, 7651–7667 (2025) DOI:10.1021/acs.jcim.5c00987