Since July 2024, AM Figueiredo has been an Auxiliary Researcher at the Coimbra Chemistry Centre (CQC-IMS) within the Department of Chemistry at the University of Coimbra. He earned his PhD in Biophysics, specializing in Biomolecular NMR Spectroscopy, from the University of East Anglia in 2011. Under the guidance of Prof. Geoffrey R. Moore and Prof. Sheena E. Radford from the University of Leeds, his research explored into the complexities of protein folding, examining how the dynamic movements of proteins across a rugged free-energy landscape relate to their biological functions, and how brief excursions to minor populated excited states influence molecular function. Following his PhD, he served as the NMR Facility Manager at the Chemistry Department of FCT-NOVA, as part of the newly established Portuguese NMR Network (PTNMR). In this position, he engaged in dissemination and training activities, lecturing in both beginner and advanced courses, co-organizing the inaugural PTNMR meeting, and authoring the first comprehensive activity report for the Portuguese national NMR infrastructure. His contributions helped pave the way for a new generation of NMR spectroscopists. In 2015, he became the Biomolecular NMR Manager at the NMR Centre of the Institute of Structural and Molecular Biology (ISMB) at University College London. There, he has participated in and collaborated on numerous scientific projects, offering not only technical expertise but also leadership, coordinating contributions from academic staff, postdoctoral researchers, and students. To date, AM Figueiredo's research has resulted in 24 peer-reviewed publications, including four as a corresponding author. Two of these publications featured as the front cover of issues. He has also supervised two MSc students and co-supervised one PhD student. AM Figueiredo, research cuts across the interface of physical chemistry and biological sciences. He has contributed experimentally to the development of new NMR methodologies, particularly to characterise biomacromolecules structurally, and dynamically [JACS (2024) 146(4):2319-24], including protein and/or RNA interactions with small ligands [Nucleic Acids Res (2023) 51(16):8774-86]. Driven by curiosity, AMFigueiredo has embarked on exploring sparsely populated, transiently formed conformations of proteins in environment-friendly designed solvents with potential applications in biochemical reactions and as pharmaceutical ingredients. Such solvents have been used to stabilise proteins and act as anti-aggregation agents. The application and development of NMR methods by which to explore sparsely populated, transiently formed conformations of proteins that are implicated in protein function and in disease. These conformers, while invisible to other biophysical methods, can be investigated at atomic resolution detail using NMR approaches. Applications to the study of protein folding, misfolding and protein aggregation in a number of disease-related systems have emerged, and atomic resolution structures of transient protein states populated to less than 1% have been described. Recently, Figueiredo has also begun developing comprehensive methodologies for NMR-based metabolomics analysis, integrating advanced AI tools to enhance these studies.