Proteins are versatile macromolecules with essential roles in all biological processes. Their structure is fundamental to their function, and proteins are not static; their conformational dynamics are continuously evolving. Thus, we assert that "Protein function is governed by both its structure and conformational dynamics."
GPCRs are a large and diverse family of membrane proteins that play a pivotal role in cellular signal transduction. These receptors are involved in a wide range of physiological processes by transmitting extracellular signals through the activation of intracellular G proteins or arrestins. Due to their critical roles, GPCRs are a major focus in drug discovery, with a substantial proportion of therapeutic agents targeting these receptors. Understanding the structure and dynamics of GPCRs is essential for advancing pharmacological research.
We investigate the conformational dynamics of GPCR signal transduction focusing on G proteins and arrestins.
Hydrogen/deuterium exchange mass spectrometry (HDX-MS) is a powerful analytical technique used to probe the dynamics and conformational changes of proteins at the molecular level. By measuring the exchange of hydrogen atoms with deuterium in a protein's backbone, HDX-MS provides detailed insights into protein folding, interaction sites, and structural stability. This method is particularly valuable for studying complex protein-ligand interactions and protein dynamics in solution. HDX-MS has become an essential tool in structural biology and drug discovery for elucidating protein behavior.
We investigate protein's conformational dynamics using HDX-MS.