XIII Congreso Nacional BIFI 2026
2026-01-14 08:00 - 2026-01-16 18:00 (Europe/Madrid) | Edificio Institutos I+D, Mariano Esquillor, 50018 Zaragoza, Zaragoza, Zaragoza, 50018, España
XIII Congreso Nacional BIFI 2026
The XIII National Conference BIFI 2025, hosted by the Institute for Bio-computation and Physics of Complex Systems of the University of Zaragoza, provides a unique occasion for participants to share their latest findings across the Institute’s diverse research fields: from Physics and Computation to Biophysics, Biochemistry, and Cell and Molecular Biology.
On this occasion, the conference will be held at the institute premises in the I+D building of Campus Río Ebro, in the University of Zaragoza, from January 14th to January 16th 2026.
As in previous editions of the BIFI National Conferences, we regard this meeting as an important occasion to strengthen our collaborations, foster new connections, and collectively advance our research. All BIFI members, especially those in the early stages of their careers, are strongly encouraged to participate and send their contributions.
More information https://bifi26.bifi.es/
MAIN TRACKS:

Biochemistry, Molecular and Cellular Biology
Physics
Biophysics
Computation

IMPORTANT DATES
Dates of the Conference: January 14th – January 16th, 2026.
Registration deadline: December 1st, 2025.
Abstract submission deadline: December 13th, 2024.
VENUE
Conference Room, Edificio I+D, Campus Río Ebro.
SPONSORS

Presentación “Acceso a recursos HPC, IA y Computación Cuántica”
2026-04-15 12:30 - 13:30 | Aula de Dirección EINA – Edificio Torres Quevedo- Campus Río Ebro, Spain
I am text block. Click edit button to change this text. Lorem ipsum dolor sit amet, consectetur adipiscing elit. Ut elit tellus, luctus nec ullamcorper mattis, pulvinar dapibus leo.

BIFI-Talk: Marcelo Guerín del IBMB-CSIC, Barcelona
2026-04-17 12:30 - 14:30 | Salon de actos del edificio I+D
BIFI-Talk: Marcelo Guerín del IBMB-CSIC, Barcelona
Título: Structural basis of glycan diversity in biological systems
Abstract
Glycosylation is one of the most prevalent posttranslational modifications of proteins and lipids. It markedly influences their structure and function, and plays a central role in nearly every aspect of biology. A deeper understanding of glycosylation —and the ability to precisely and rationally modulate it— are essential for advancing our fundamental biological knowledge and for developing innovative therapeutics across a wide range of human diseases.
In this talk, I will present our recent findings and advances in the following research areas:
(i) Bacterial cell envelope biosynthesis and remodeling, and its impact in host-pathogen interactions and vaccine development. Surface glycan polymers are crucial virulence factors of pathogenic bacteria. We identified enzymatic machineries assembling these polymers, key for developing novel antimicrobials and enzyme-based vaccine synthesis protocols (Sci. Adv. 7:eabj4565, 2021; Nat. Chem. Biol. 19:795-796, 2023; Nat. Commun. 14:6694, 2023; Nat. Commun. 15:5740, 2024; Nat. Chem. Biol. 21:120-130, 2025).
(ii) Unveiling the role of gut microbiota glycan processing machinery in human health and disease. The gut symbiotic microbiota provides the complementary enzymatic machinery necessary to orchestrate the depolymerization of glycan structures into their sugar components that otherwise could not be processed by the host. We identified novel enzymatic activities and substrate specificities associated to N- and O-linked glycans breakdown, including FucOB from Akkermansia muciniphila capable of converting universal O red blood cells and human kidney tissues into the rare Bombay phenotype.
(iii) Glycoprotein folding and quality-control mechanisms in human diseases. The endoplasmic reticulum (ER) glycoprotein folding quality control protein machineries survey glycoprotein folding in the early secretory pathway. We unveiled the structural and mechanistic aspects of the ER folding sensor UDP-glucose glycoprotein glucosyltransferase (UGGT). This allows us to define the molecular basis of a novel congenital disorder of glycosylation (CDG) disease, characterized by significant neurological dysfunction.
In our research, we are using a truly multidisciplinary approach. To determine high-resolution structures, we employ X-ray crystallography and single particle cryo-electron microscopy. To obtain mechanistic insight, we combine structural studies with molecular biology, protein/membrane biochemistry/biophysics and AI-driven computational methods. These approaches are frequently integrated with collaborative efforts in genomics, transcriptomics, proteomics, cell biology, synthetic organic chemistry and NMR spectroscopy.
