Steve Harborne PhD

Head of Membrane Protein Science

Steve has extensive skills in bioinformatics, molecular biology, cell culture, protein purification and analysis.

Steve Harborne PhD Specialist in Membrane Protein Biochemistry

More about Steve

Steve is interested in protein biochemistry, bikes and beer (not necessarily in that order). His academic journey begun at the University of Sheffield where, for better or worse, he discovered the world of protein biochemistry and structural biology. He thought it would be a great idea to do a PhD in this field, but not content on a regular difficulty PhD, he pitted himself against the formidable challenge of membrane protein structural biology. Following four years of caffeine fueled hard graft he graduated from the University of Cambridge, taking his hard-won skills to the University of Leeds to work on membrane proteins for a bit longer. Finally, after 11 years at Uni he decided it was time to stop being a student and find a real job (and possibly work on less obstinate projects). With a couple of stops along the way in Big Pharma such as GSK and Novartis, he found his way to Peak Proteins. When not heading up the Peak Proteins peloton, Steve tries his hand at all stages of the Peak Proteins workflow: from expression, through purification, all the way to crystallisation and structure determination. Membrane proteins forever remain in his heart.

Notable Publications (click to view)

Calcium-regulated mitochondrial ATP-Mg/Pi carriers evolved from a fusion of an EF-hand regulatory domain with a mitochondrial ADP/ATP carrier-like domain
IUBMB Life 2018 70(12). pp. 1222-1232. doi: 10.1002/iub.1931
Harborne, SPD and Kunji, ERS.

Revolutionising the design and analysis of protein engineering experiments using fractional factorial methods
BioRxiv 2018 doi: https://doi.org/10.1101/298273
Harborne SPD, Wotherspoon D, Michie J, McComb A, Kotila T, Gilmour SG and Goldman A.

A simple strategy to determine the potassium-dependency of membrane-bound pyrophosphatases
Methods in Enzymology 2018 607 pp131-156. doi: 10.1016/bs.mie.2018.04.018
Strauss J, Wilkinson C, Harborne SPD, and Goldman A.

Defining dynamics of membrane-bound pyrophosphatase by experimental and computational single-molecule FRET
Methods in Enzymology 2018 607 pp 93-130. doi: 10.1016/bs.mie.2018.04.017.
Harborne SPD, Strauss J, Turku A, Watson MA, Tuma R, Harris SA and Goldman A.

Pacing across the membrane: the novel PACE family of efflux pumps is widespread in Gram-negative pathogens
Research in Microbiology 2018 169(7-8)pp 450-454 doi: 10.1016/j.resmic.2018.01.001.
Hassan KA, Liu Q, Elbourne LDH, Ahmad I, Sharples D, Naidu V, Lam Chan C, Li L, Harborne SPD, Pokhre A, Postis VLG, Goldman A, Henderson PJF and Paulsen IT.

Calcium regulation of the human mitochondrial ATP-Mg/Pi carrier SLC25A24 uses a locking pin mechanism
Scientific Reports 2017 7 p. 45383 doi: 10.1038/srep45383
Harborne SPD, King MS, Crichton, PG and Kunji ERS.

Insights into the mechanism of membrane pyrophosphatases by combining experiment and computer simulation
Structural Dynamics 2017 4. doi: 10.1063/1.4978038.
Shah NR, Wilkinson C, Harborne SPD, Turku A, Li K-M, Sun Y-J, Harris S and Goldman A.

Employee Spotlight

What work do you do at Peak Proteins?

With the team at Peak Proteins being relatively small, I try my hand at lots of different things throughout the protein delivery pipeline. I’ve helped write customer quotes, expressed protein, purified and crystallised bucket loads of protein and helped solve an X-ray structure or two. However, my main speciality is working with membrane proteins, and I’ve started to focus on building Peak Protein’s capabilities around generating and working with these tricky targets.

What did you do before joining Peak Proteins?

Before Peak Proteins I was an academic scientist working on membrane protein structure and function. I did my PhD in Cambridge and a Post Doc at the University of Leeds.

What was your favourite subject at school?

It was a close tie between Science and Art. I love understanding how and why things work the way they do, and I also enjoy symmetry, patterns and order. This is probably why I’m a structural biologist, always trying to determine beautiful protein structures.

Who is your scientific hero and why?

The Nobel Prize winner Peter Mitchell who hypothesised the chemiosmotic theory, which is a description of how a proton motive force – potential energy stored as a difference in concentration and charge of protons across a biological membrane – can be used to drive biochemical reactions such as the synthesis of ATP. His work was ridiculed at first as his theory did not fit the biochemical schemes of cellular metabolism known at the time from glycolysis and he was forced to self-publish all of his work as the academic journals would not accept it.

What interested you about Peak Proteins which prompted you to join the business?

After realising an academic career wasn’t what I wanted long term, I was looking for a change of pace that would allow me to continue working on interesting challenges in science but cut out all of the frustrations that go along with working in academic science. After experiencing work in a big pharmaceutical company during my undergraduate placement year, I didn’t feel like that was the right fit either. Instead, Peak Proteins looked to offer the best of both worlds: a collaborative and dynamic work environment in a small team without the need to constantly apply for grant funding.