Вьегас Альдино

I graduated in Biochemistry in Faculdade de Ciências da Univ. de Lisboa and I received my Ph.D. in Structural Biochemistry in 2012 by Faculdade de Ciências e Tecnologia da Univ. Nova de Lisboa (FCT-NOVA), having been awarded the António Xavier Prize, for the Best National Thesis in the field of NMR (2013). My research focused on the study of protein-ligand interactions and protein structure by NMR spectroscopy, X-ray crystallography, molecular biology and molecular docking. In 2012 I attained a position as a Scientific Officer at Fundação para a Ciência e a Tecnologia, and, in Sep. 2013, to embrace a new scientific challenge on the study of membrane proteins (MP), I took a research position in Germany (HHU Duesseldorf) to study MP structure and function by NMR. Shortly after, I was awarded a Marie Sklodowska-Curie Individual Fellowship to study the Epidermal Growth Factor Receptor (EGFR). This granted me strong skills in the field of MP NMR, membrane mimetics (nanodiscs) and pulse sequence development (UTOPIA-NMR). The methods developed and the results obtained advanced both the field of NMR for the study of MPs, and the current knowledge on key aspects of EGFR signaling. During this period, I was involved in teaching and co-supervision of master and Ph.D. students and had the opportunity to collaborate with experts in areas from chemistry, biochemistry to NMR engineering. Since Nov. 2017, I am working as a researcher in FCT-NOVA and my research is focused on the integration of NMR with other structural biology techniques to study protein-ligand interactions in complex systems and the effect of charged metabolites on protein folding and stability. In 2020 I was a awarded an Assistant Researcher contract (2020.00043.CEECIND) in the 2020 Individual Call to Scientific Employment Stimulus to study the molecular basis for ligand recognition of the human norepinephrine transporter. To complement this contract, in 2021 I was awarded an exploratory project (EXPL/BIA-BQM/0011/2021) to study ligand interaction and allosteric modulation of the same transporter.