Douglas Ferreira,Newcastle University,UK

https://umr1087.univ-nantes.fr/medias/photo/photo_1793978807827
  • On 30 November 2026
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  • 14h00

Cryo-EM and AlphaFold: Applications in Structural Biology

Cryo-EM and AlphaFold: Applications in Structural Biology

Douglas Ferreira, PhD,
Research Associate

Biography

Dr Douglas Ferreira is a Research Associate at Newcastle University, where he uses cryo-electron microscopy (cryo-EM) to study protein complexes involved in cell cycle regulation and drug discovery. He completed his DPhil in Clinical Medicine at the University of Oxford in 2024, investigating the structure of human methionine synthase. His research combines structural biology, biophysical assays, and computational approaches (such as AlphaFold) to understand protein function and interactions. Earlier in his career, he worked on the immunological characterisation of yellow scorpion's (Tityus serrulatus) toxins. His current work focuses on using structural information to investigate protein–ligand and protein-protein interactions to support drug discovery.

Abstract 

Advances in cryo-electron microscopy (cryo-EM) and protein structure prediction have expanded the ability to investigate proteins. Human methionine synthase (MTR) provides an example of how these approaches can complement each other. Cryo-EM enabled the determination of high-resolution structures of distinct regions of MTR, providing insights into its conformational flexibility and molecular function. AlphaFold was further applied to investigate interactions between MTR and its protein partners, supported by biochemical experiments. These findings highlight the potential of combining experimental and computational approaches to study protein structure, conformational variability, and molecular interactions, while also illustrating their current limitations.
Updated on 06 November 2026.