Marcelino Arciniega Castro

Marcelino Arciniega Castro

Bioquímica y Biología Estructural

Lab 102 Oriente

Tel. +52 55 562 257 03

Intereses de Investigación

The goal of the lab is to establish a multidisciplinary work environment where physics, chemistry, mathematics and computational sciences converge towards structural biology. Using computational tools we aim to elucidate function-structure relationships that govern cellular processes at molecular level. Conformational changes, allosteric signals and protein-ligand interactions are just some of the processes that can be studied in biological macromolecules in the computational manner. The computational structural biology complements experimental studies not only by generating new hypotheses to be tested in the lab, but also by providing valuable interpretations of complex experimental results.

We are interested in:

Study of conformational changes using molecular dynamics techniques such as Metadynamics and Markov State Models.

Development of algorithms for inhibitor virtual screening and design using machine learning techniques.

Development of algorithms for the study of protein complex formation using protein-protein docking.

Trayectoria profesional

Investigador Asociado C, SNI I

Instituto de Fisiología Celular (desde 2015)

Universidad Nacional Autónoma de México

Posdoctorados y estancias

Prof. Dr. Robert Huber (2014-2015)

Max Planck Institut für Biochemie, Munich, Alemania

Formación académica

Dr. en Ciencias Naturales (2009-2014)

Technische Universität München, Alemania

Maestría en Física Médica (2006-2009)

Instituto de Física UNAM, México DF, México

Lic. en Física (2002-2006)

Universidad de Guadalajara, Guadalajara, Mexico

Líneas de Investigación

Aperture of 20S Proteasome´s central cavity : The cell must adapt its protein levels in response to many conditions such as oxidative stress, cellular differentiation or changes in the flux of nutrients. Eukariotic cell use the Ubiquitin Proteasome System (UPS) as the main degradation pathway to adjust proteins levels. Protein degradation occurs in the 20S Proteasome - a cylindrical macromolecular complex formed by 28 subunits arranged in 4 stacked heptameric rings. The central cavity of this complex harbours catalyticly active sites that coordinate protein degradation. This process is highly regulated by the opening and closing of the central cavity. A detailed study of the aperture mechanism allows better understanding of the 20S Proteasome function and also provides new possibilities to regulate the UPS.