Dr Manuel Müller MRSC

Winner: 2021 Chemistry Biology Interface Division early career award: Norman Heatley Award

King's College London

For contributions to the field of posttranslational modifications, especially the use of protein chemistry to gain insight into molecular mechanisms of epigenetics processes and cancer.

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Chemistry is a fascinating subject that helps you to understand the world around you and enables you to contribute to improving it.

Proteins are molecular machines that carry out many essential functions in life. Just like macroscopic machines, proteins are controlled by on/off switches, called posttranslational modifications. Dr Müller's research aims to understand how these molecular switches operate and how failures in switching behaviour leads to disease.

Dr Müller and his team are able to measure the properties of proteins in their on and off states by using chemistry to synthesise proteins with defined posttranslational modifications. At the same time, his team is developing new chemistries to find previously unknown types of switches.

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Dr Manuel Müller studied biochemistry at ETH Zürich. He stayed on to pursue a PhD in biological chemistry with Professor Don Hilvert. His work on model systems of primordial enzymes was supported by a fellowship from the Scholarship Fund of the Swiss Chemical Industry and awarded the ETH Medal. He then joined Professor Tom Muir’s lab at Rockefeller as a postdoctoral fellow (Swiss National Science Foundation) and moved with the lab to Princeton. There he developed and applied chemical biology tools to study chromatin-modifying enzymes and how these enzymes contribute to epigenetic phenomena and diseases. In 2016, he joined the recently re-established chemistry department at King’s College London as a Wellcome Trust/Royal Society Sir Henry Dale Fellow.

His interdisciplinary lab investigates the function of post-translational modifications (PTMs) and how these molecular on/off switches control cellular life and death decisions. His team is particularly interested in an unusual class of PTMs: those that occur on the polypeptide backbone. By using synthetic protein chemistry and developing bespoke (bio)chemical technologies to interrogate backbone PTMs, he aims to delineate the unique mechanisms that these modifications contribute to protein structure and function.

Q+A

How did you first become interested in chemistry?

I set out to study biology with chemistry because I wanted to learn more about the molecular basis of life. Dolly the sheep had just been cloned, so there was a lot of discussion about this rather enigmatic topic at the time. At university, I was drawn to chemistry classes because I was fascinated by the logic of physical and organic chemistry but it took me a few years to appreciate that much of biological signalling is also governed by chemistry. This realisation sparked my continuing interest in the chemistry of proteins.

Who or what has inspired you?

I’ve been very fortunate to have had mentors and colleagues who truly cared about science. There was always someone around to discuss ideas with and I’ve had the freedom to explore the questions that I found interesting.

What motivates you?

One of the nicest perks of a research career is that we get to learn something new every day. By working with creative students and colleagues, I never run out of inspiration.

What advice would you give to a young person considering a career in chemistry?

Chemistry is a fascinating subject that helps you to understand the world around you and enables you to contribute to improving it. Keeping an open mind to neighbouring disciplines will enhance your ability to solve increasingly complex problems.

What has been a highlight for you (either personally or in your career)?

Being able to collaborate with scientists across disciplines, including medical doctors, has been extremely enriching on both a personal and a professional level. And it has highlighted to me the strengths of working as a team and that basic research contributes to applied science in unexpected ways.

What is your favourite element?

Sulfur, because it provides the unique reactivities of my favourite amino acid, cysteine. Over the years, I’ve gotten over the unpleasant smell of the sulfur compounds we use in the lab and found it quite useful as a reporter for good lab practice when training students.