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Dan S. Tawfik (Born on 28 May, 1955) is a Israeli biochemist. His research regards enzymes, and enzyme evolution in particular.

Biography
Dan was born in Jerusalem, Israel, on 28 May 1955. He received his B.Sc. in chemistry and biochemistry (1988) and MSc in biotechnology (1990) from the Hebrew University in Jerusalem, and his PhD from the Weizmann Institute of Science (1995). After two years of postdoctoral research at Cambridge University (UK) and the at Medical Research Council (MRC) Centre for Protein Engineering, he became a senior research fellow at Sidney Sussex College]] and at the MRC Laboratory of Molecular Biology, where he was appointed group leader in 1999. He joined the Weizmann Institute faculty in 2001, and holds the Nella and Leon Benoziyo Professional Chair.

Career and research
Tawfik developed in vitro compartmentalization (jointly with Andrew D. Griffiths ). This technology enables the compartmentalization of single DNA/RNA molecules in emulsion droplets, thus providing cell-like compartment, in which genes can be replicated, transcribed and translated. This technology allowed directed enzyme evolution to be performed without the involvement of living cells, and also became the basis of massive parallel sequencing methods such as 454 sequencing  or SOLID, and of Digital polymerase chain reaction.

Tawfik has been one of the earliest contributors to the study of enzyme promiscuity and its role in enzyme evolution. He established the link between the conformational diversity of proteins and their promiscuity, demonstrated the evolvability of promiscuous protein functions (the ability of mutations to dramatically enhance a promiscuous activity with minor effects of the protein’s original function ), and the role of promiscuity in the evolution of pesticide degrading enzymes. His has also addressed the evolutionary trajectories that lead to new enzymes, and the link between protein folding, stability and evolvability.

His research on the emergence of the first enzymes is establishing the roots of the most common enzyme lineages, the Rossmann and Rossmann NTPases, in simple polypeptides  , and suggested ornithine  as the first cationic amino acid , demonstrated the evolvability of promiscuous protein functions (the ability of mutations to dramatically enhance a promiscuous activity with minor effects of the protein’s original function.

Awards and honours
• The Wolgin Prize for Scientific Excellence (2007)

• The Weizmann Prize from the Tel Aviv municipality (2007)

• EMBO member (2009)

• Teva Award for Excellence in Memory of Eli Hurvitz (2013)

• The ECI Enzyme Engineering Award (2015)

• The EMET Prize in Life Sciences (2020)