Watch Dek introduce the work we do here in the Woolfson group at Bristol on understanding the protein folding problem and de novo protein design

We're delighted to announce that our conference "Protein Evolution, Design and Informatics Edinburgh 2026" will be running from the 13th-15th of May. Register interest here and please retweet!

Designing proteins from scratch opens exciting new possibilities for solving global challenges in health and sustainability. That is why we are funding an ambitious new Center for Protein Design at @koebenhavns_uni. Led by Professor Dek Woolfson, world-renowned in this field,

From sequence–structure analysis of natural 3HBs, we derived polar layer packing rules + charge patterning to design 2x ABN heterotrimer peptides, seeding hyperstable, monomeric proteins in clockwise & anticlockwise topologies by precisely controlling helix–helix interfaces.

New paper from our group combines rational and computational design to build antiparallel 3-helix bundle (3HB) assemblies and single-chain proteins with defined topology and tunable thermal stability. 🧩 https://t.co/LX0MMN8r74

This dual base will allow us to build a strong bridge between the two institutions, facilitating the exchange of ideas, people, and expertise in protein design. We look forward to deepening our links with Copenhagen and to contributing to the CPD’s exciting mission!

As part of this new chapter, our research group will expand its activities to Copenhagen, forming a joint presence across both sites. We will continue to operate in Bristol, while establishing new lines of research and collaborations within the CPD.

As part of this, Dek will share his time between Bristol and Copenhagen, remaining a Professor at the University of Bristol, helping maintain and grow these links.

To support international exchange and mobility, the CPD will establish a network of Research Spokes, with the first based at the University of Bristol. This will strengthen and expand ongoing collaborations, serve as a platform for joint research, and shared training initiatives.

Dek has driven partnerships across chemistry, biochemistry, cell biology, materials science, and computational design. This collaborative ethos will be at the heart of the CPD, fostering strong ties across faculties, departments, and institutions.

A key strength of the CPD will be its deep commitment to interdisciplinary and collaborative research, both within Denmark and internationally. Dek brings a wealth of experience in building and leading such efforts, notably through BrisSynBio and the Bristol BioDesign Institute.

The CPD will span the Faculty of Science and the Faculty of Health and Medical Sciences at UCPH, with core activities in the Department of Biology and the Department of Drug Design and Pharmacology, and additional contributions from Departments of Chemistry and Computer Science.

It will be a world-leading hub for de novo protein design, advancing fundamental understanding of protein structure and function while developing novel proteins to address challenges in healthcare, biotechnology, and sustainability.

The Centre is supported by a 700 million DKK (≈£80 million) grant from the Novo Nordisk Foundation, awarded for an initial period of seven years. The CPD will officially launch in August 2025.

We are thrilled to announce that Professor Dek Woolfson has been appointed Director of the Novo Nordisk Foundation Centre for Protein Design (CPD) at the University of Copenhagen. https://t.co/U2YW6oiBUl

🚛🧬 New paper on rXiv! We reveal how cargo binding activates kinesin-1 by dislocating the TPR shoulder — a key structural switch that unlocks motor movement. Happy reading! 🔗 https://t.co/GW9b8jUOpY

This work was highlighted on APS:

Read more here:

Another publication in collaboration with Tom Oliver's group in @BristolChem We harness de novo α-helical barrels as "molecular flasks" to bind and orient small molecules in aqueous solution. Using FRET and photodimerization, we showcase the potential for templating new chemistry

Read more here:

🔬 New paper from our lab! We explored peptide exchange dynamics in de novo coiled-coil assemblies, from dimers to heptamers, revealing both faithful and promiscuous behaviours. Using a new fluorescence-based assay, we uncovered design strategies to enhance orthogonality.