Ricerc@Sapienza

The Lab is runed by 3 peers: Carlo Travaglini Allocatelli, Giorgio Giardina and Adele Di Matteo

WHAT: The Lab is focused on the determination of 3D protein structures at the atomic level and on the analysis of protein folding and miss-folding process including beta-amyloid formation. 

WHY: By analysing the folding mechanism and the native structure of proteins we can provide a basic understanding of the molecular mechanisms governing a specific genetic disease, as well as host pathogen interactions. We aim at a structure based understanding of how specific proteins work and interact with ligands and/or other biological macromolecules. These structural and mechanistic information can then be exploited to develop new therapeutic and antimicrobial strategies to target these proteins or their complexes. 

HOW: Target proteins are heteroexpressed and purified by standard techniques. Protein structures are determined by X-ray diffraction and cryo-EM techniques. Protein folding studies are performed by standard techniques which include the use of circular dichroism; UV-vis and fluorescence spectroscopy; rapid kinetics apparatus.

INTERNSHIP: We are always looking for curious students, if you want to work with us for your bachelor or master's degree final lab training, drop us an email.

During their internship students will learn:

• Expression and growth of recombinant proteins
• Purification of proteins by affinity tags and various chromatographic techniques
• Cloning and mutagenesis (depends on the project)

Additionally, and depending on their project, some of the following protein science techniques:

• Biochemical characterization, stability study, binding affinity and/or kinetic study: UV-Vis, Fluorescence, Circular dichroism, Rapid kinetics (stopped flow), Mass photometry, SPR, ITC
• Structural study: Crystallization of proteins or preparation of grids for Cryo-EM, data analysis, model building, structure-function analysis