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Dr Sebastian Ahnert

Dr Sebastian Ahnert

Career Development Fellow

Sainsbury Laboratory
University of Cambridge
47 Bateman Street
Cambridge CB2 1LR

Office Phone: +44(0)1223 761148


Sebastian Ahnert read physics (BA Hons) and mathematics (Part III) at Sidney Sussex College, Cambridge before completing a PhD in the Theory of Condensed Matter group at the Cavendish Laboratory under Professor Mike Payne. During his PhD he became interested in the growing interface between statistical physics and biology and afterwards took up a postdoc at the Institut Curie in Paris. He returned to the Cavendish for a Leverhulme Early Career Fellowship, during which he spent six months at Northeastern University in Boston visiting the group of Professor Albert-Laszlo Barabasi. In 2009 he took up a Royal Society University Research Fellowship at the Cavendish Laboratory to work on quantitative measures of structural complexity in self-assembling systems. He started a joint position between the Sainsbury Laboratory and the Cavendish Laboratory in 2016.

Research Interests

My main research interests lie on the interface of theoretical physics, biology, mathematics and computer science. I am particularly interested in using algorithmic descriptions of structures and functional systems in order to quantify and classify their complexity. Examples of the application of such approaches include pattern detection in gene expression data, the classification of protein quaternary structure, the structure of genotype-phenotype maps and the identification of large-scale features in complex networks. Connected to this I am also interested in interdiscliplinary applications of network analysis, particularly in the context of digital methods and large-scale data analysis in the humanities. 

Key Publications

S. E. AhnertStructural properties of genotype-phenotype maps, 
Journal of the Royal Society Interface 14, 20170275 (2017) 

S. E. Ahnert, J. A. Marsh, H. Hernandez, C. V. Robinson, S. A. Teichmann 
Principles of assembly reveal a periodic table of protein complexes 
Science 350, 1331 (2015)

 J. Marsh, H. Rees, S. E. Ahnert, S. A. Teichmann 
Structural and evolutionary versatility in protein complexes with uneven stoichiometry Nature Communications 6, 6394 (2015)

M. Taylor-Teeples, L. Lin, M. de Lucas M, G. Turco, T. W. Toal, A. Gaudinier, N. F. Young, G. M. Trabucco, M. T. Veling, R. Lamothe, P. P. Handakumbura, G. Xiong, C. Wang, J. Corwin, N. Tsoukalas, L. Zhang, D. Ware, M. Pauly, D. J. Kliebenstein, K. Dehesh, I. Tagkopoulos, G. Breton, J. Pruneda-Paz, S. E. Ahnert, S. A. Kay, S. P. Hazen, S. M. Brady 
An Arabidopsis Gene Regulatory Network for Xylem Specification and Secondary Wall Biosynthesis Nature 517, 571 (2015)

S. F. Greenbury, I. G. Johnston, A. A. Louis, S. E. Ahnert A tractable genotype-phenotype map modelling the self-assembly of protein quaternary structure Journal of The Royal Society Interface 11, 20140249 (2014)

J. A. Marsh, H. Hernandez, Z. Hall, S. E. Ahnert, T. Perica, C. V. Robinson, S. A. Teichmann Protein complexes are under evolutionary selection to assemble via ordered pathways Cell 153, 461 (2013)

M. A. Moreno-Risueno, J. M. Van Norman, A. Moreno, J. Zhang, S. E. Ahnert, P. N. Benfey Oscillating Gene Expression Determines Competence for Periodic Arabidopsis Root Branching Science 329, 1306 (2010)

S. E. Ahnert, I. G. Johnston, T. M. A. Fink, J. P. K. Doye, A. A. Louis Self-assembly, modularity and physical complexity Physical Review E 82, 026117 (2010)

S. E. Ahnert, K. Willbrand, F. C. S. Brown, T. M. A. Fink Unbiased pattern detection in microarray data series Bioinformatics 22, 1471 (2006) 

Ahnert research imageClick here for a larger version of this image.

Three possible evolutionary steps give rise to the vast majority of observed protein quaternary structure. Each step corresponds to the evolution of an interface. The three types of interfaces are: (i) homomeric isologous, meaning a symmetric interface, (ii) homomeric heterologous, meaning an asymmetric interface between subunits of the same type, and (iii) heteromeric heterologous, meaning an asymmetric interface between subunits of different types. By considering the different ways in which these interfaces can be distributed across subunits we can classify known protein complex topologies into a 'periodic table' and predict novel topologies that are likely to be discovered in the future.


Research supported by grants from:

Royal Society excellence in science