Publications:

1.       Toth-Petroczy A*, Palmedo P*, John Ingraham JI, Thomas A. Hopf TA, Berger B, Sander C, Marks DS. Structured states of disordered proteins from genomic sequences. Cell 2016, 167(1):158-70.

2.       Rockah-Shmuel L, Toth-Petroczy A, Sela A, Wurtzel O, Sorek R and Tawfik DS. The Occurrence and Bypass of Frame-shifting Insertion-Deletions (InDels) to give Functional Proteins are correlated. PloS Genetics 2013 (10) e1003882

3.       Dellus-Gur E*, Toth-Petroczy A*, Elias M, Tawfik DS. What makes a protein fold amenable to functional innovations? Fold polarity and stability trade-offs. J Mol Biol 2013; 425(14):2609-21.

4.       Toth-Petroczy A and Tawfik DS. Protein insertions and deletions enabled by neutral roaming in sequence space. Mol Biol Evol 2013; 30(4):761-71.

5.       Tóth-Petróczy A and Tawfik DS. Slow protein evolutionary rates are dictated by surface-core association. PNAS 2011, 108(27):11151-6.

Abstract:

Protein sequence space is vast, the possibilities are astronomical, yet only a tiny fraction of it is sampled by existing proteins. We mine evolutionary information from millions of genomes to understand how protein families evolve, and what rules govern their functional and structural divergence. We focus not only on genetic mutations but also on phenotypic mutations, i.e. mutations introduced by transcriptional and translational machinery. We wish to answer how proteins remain robust to mutations and facilitate innovations at the same time. We combine bioinformatics, modelling and experimental evolution to answer fundamental questions about molecular evolution.

Everybody is very welcome!