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A Chemical Approach to Protein Design—Template‐Assembled Synthetic Proteins (TASP)
Author(s) -
Mutter Manfred,
Vuilleumier Stéphane
Publication year - 1989
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.198905353
Subject(s) - folding (dsp implementation) , protein design , protein folding , synthetic biology , protein engineering , chemistry , chemical synthesis , computational biology , nanotechnology , computer science , combinatorial chemistry , protein structure , biology , biochemistry , engineering , materials science , electrical engineering , in vitro , enzyme
Advances in methodology in both chemistry and molecular biology allow us to take a fresh look at protein science. Chemical synthesis of peptides and site‐directed mutagenesis are now standard research tools, paving the way for the construction of new proteins with tailor‐made structural and functional properties. The decisive hurdle on the way lies not in the synthesis of the molecules proper but rather in a better understanding of the complex folding pathways of polypeptide chains into spatially well‐defined structures. Can the chemist use his synthetic tools to bypass the notorious “folding problem?” In this article, we present a new approach developed in our laboratory, which opens a chemical route to artificial proteins with predetermined three‐dimensional structures, allowing a first step towards the synthesis of new proteins with functional properties.