Ομάδα Δομικής Βιολογίας
Τμήμα Βιοτεχνολογίας, Γεωπονικό Πανεπιστήμιο Αθηνών
Επικ. Καθ. Πέτρος Γκιάστας
Structural Biology Group
Department of Biotechnology, Agricultural University of Athens
Ομάδα Δομικής Βιολογίας
Τμήμα Βιοτεχνολογίας, Γεωπονικό Πανεπιστήμιο Αθηνών
Structural Biology Group
Department of Biotechnology, Agricultural University of Athens
Part of the Genetics Laboratory, Department of Biotechnology, School of Applied Biology and Biotechnology at the Agricultural University of Athens.
Welcome to my personal page. I am Petros Giastas, a structural biologist and biochemist with a strong interest in understanding how proteins work at the molecular level. My research and teaching revolve around biochemistry and the relationship between protein structure and biological function. I work primarily with proteins, receptors and enzymes, aiming to uncover how their structures dictate their roles in health and disease. Find me also in Google Scholar, Scopus, Orcid, ResearchGate and LinkedIn. If you are new in this website, do not miss our handy wet lab calculation tools, the protein crystallization tool and the buffer preparation tool.
Scientific Interests
Protein Structure and Function
Proteins are the molecular machines of life. Their three-dimensional structures are the key to understanding how they recognize ligands, catalyze reactions, and transmit signals across membranes. Even small structural details—like the orientation of a side chain or the flexibility of a loop—can determine whether a protein is active, inactive, or misregulated in disease.
Studying protein structures helps us reveal conserved motifs and mechanisms that are hidden at the sequence level but become evident once the molecule is visualized in 3D.
X-ray Crystallography and Structural Biology Methods
X-ray crystallography remains one of the most powerful tools for high-resolution visualization of proteins, enabling us to capture molecular details down to the atomic level.
I am also interested in the complementarity of structural biology methods—such as cryo-electron microscopy, NMR spectroscopy, and computational approaches—to study proteins that are dynamic, large, or otherwise difficult to crystallize.
Structure-Based Drug Design
A central aspect of my research is the rational design of small molecules that modulate protein activity. By knowing the 3D structure of a protein, we can identify binding pockets, predict how ligands interact with the active or allosteric sites, and design compounds with higher affinity, selectivity, and potency. This approach bridges fundamental research and therapeutic application, providing insights into enzyme regulation, receptor signaling, and drug discovery.
Molecular Recognition
My teaching and research also focus on how biological molecules specifically recognize each other—whether it’s a protein binding to DNA, an antibody recognizing an antigen, a receptor engaging a ligand or an enzyme binding its substrate. Understanding molecular recognition at the structural level explains specificity, efficiency, and regulation in cellular systems.
Protein Folding and Dynamics
Proteins are not static objects. Their biological function often depends on conformational changes, folding pathways, and dynamic equilibria between different states. I am especially interested in how proteins fold in their favorable state, how the dynamics relate to enzymatic activity and how small molecules or chaperones can shift conformational landscapes to regulate function.