Unfolding the secrets of biomolecules
Professor Teresa Carlomagno is Director of the National Biomolecular NMR facility and Professor of Integrative Structural Biology in the School of Biosciences. She uses Nuclear Magnetic Resonance (NMR) spectroscopy to reveal not only
the three-dimensional structures of RNAs, proteins, and their complexes, but also their dynamics and interactions in biologically relevant environments.
What is your aim in biosciences?
I want to uncover and understand the struc- tural basis of important biological systems and processes. My aim is not only to solve static structures of proteins, RNAs, and their com- plexes, but also to explore how these mole- cules behave in action: how they change shape during function, interact with partners, and participate in regulation. My research forms the molecular foundation for interpreting the chemistry of life processes and is essential to modern biotechnology and drug discovery.
Why is NMR useful for your research in biology?
NMR signals stem from individual atoms and are sensitive to the local chemical and spatial environment, allowing researchers to deter- mine the 3D structure of molecules and probe their dynamics. Unlike methods that require crystallisation, NMR works in both solution and solid states, making it especially valuable for studying large, flexible, or disordered biological systems under near-physiological conditions.
Where does your research group lead in the field?
Beyond structural determination, we lead efforts to uncover the structure–dynamics– function relationships of biomolecules. This includes investigating how flexible or disor- dered regions contribute to regulation, how conformational changes occur during function, and how molecular recognition is mediated in dynamic contexts. Our approach expands clas- sical static structures to dynamic behaviour.
What makes your research distinctive?
My research benefits from access to the state- of-the-art NMR spectrometers at the national Henry-Wellcome Building for Biomolecular NMR at the University of Birmingham. We will soon have the world’s highest magnetic field 1.2 GHz system equipped with a 28.2 Tesla magnet. The high field provides high sensitivity and resolution, allowing us to study large or complex biomolecules like membrane proteins, large RNA-protein complexes, or disordered domains. Our group pioneered solid-state NMR methods to determine high-resolution RNA structures, enabling the analysis of large systems not accessible to other techniques. We also integrate NMR with complementary tools such as molecular biology, computation- al modelling, and other biophysical methods
to create a holistic picture of structure and function.
How does this research translate into real-world applications?
A key application area is rational drug design. By understanding the 3D structure and dynamic interactions of RNAs and protein–RNA complexes, we can identify and optimise small molecules that block disease-related interac- tions—for example, those involved in cancer, viral replication, or splicing defects. We also work on regulatory domains in proteins, whose switchable structural states make them prom- ising therapeutic targets. Our research thus bridges fundamental molecular understanding with translational aims in medicine and bio- technology.
Nuclear Magnetic Resonance (NMR) is a spectroscopic technique that detects signals from specific atomic nuclei in a sample. These nuclei behave as tiny magnetic dipoles, and when subjected to radiofrequency irradiation in the presence of a static magnetic field, they undergo resonant transitions that emit signals containing detailed chemical and structural information. The University of Birmingham hosts more than a dozen NMR spectrometers across the Schools of Biosciences, Chemistry, Civil Engineering, and Physics and Astronomy.
By understanding the 3D structure and dynamic interactions of RNAs and protein–RNA complexes, we can identify and optimise small molecules that block disease-related interactions— for example, those involved in cancer, viral replication, or splicing defects.
