PROTEIN STRUCTURE AND DYNAMICS, FUNCTION AND ASSEMBLY
IN HEALTH AND DISEASE
IN HEALTH AND DISEASE
We determine protein 3D structures at atomic resolution using solution state NMR spectroscopy.
We leverage from NMR relaxation techniques to investigate protein dynamics and their behavior at different time scales, specifically focusing on inter-domain motion that mediate protein function and assembly. We travel from atomic resolution to the supramolecular world by identifying the structural characteristics and factors involved in the formation of large, supramolecular protein assemblies.
Most of our research projects involve biomacromolecules that participate in the inflammatory process in the organism and in the necessary death of damaged, old or infected cells (programmed cell death). The main goal of our research interests lies in deciphering the underpinnings of inflammation and cell death to be able to understand the molecular bases of health and disease.
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Our lab uses NMR and fluorescence spectroscopy combined with computational docking to study protein/protein interactions that govern the mechanisms of key biological processes.
Our studies help to define with detail the interacting surfaces for the rational design of therapeutics targeted at interfering with these interactions and modify protein function. These studies typically provide averaged information of biomolecular behavior, thus missing important cues from the individual components. Biomacromolecules may act as independent, single activators that prompt a cascade of subsequent events. With the aim of gaining information on protein function and conformation at the single molecule level, we use confocal microscopy in concert with optical tweezers.
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