Minimalist de novo Design of Protein Catalysts.

ACS Catalysis
Liam R MarshallI V Korendovych

Abstract

The field of protein design has grown enormously in the past few decades. In this review we discuss the minimalist approach to design of artificial enzymes, in which protein sequences are created with the minimum number of elements for folding and function. This method relies on identifying starting points in catalytically inert scaffolds for active site installation. The progress of the field from the original helical assemblies of the 1980s to the more complex structures of the present day is discussed, highlighting the variety of catalytic reactions which have been achieved using these methods. We outline the strengths and weaknesses of the minimalist approaches, describe representative design cases and put it in the general context of the de novo design of proteins.

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Citations

Feb 24, 2021·The Journal of Physical Chemistry. a·Wiktoria JedwabnyKonrad Patkowski
Feb 27, 2021·Journal of the American Chemical Society·Elise A NaudinVladimir Torbeev
Apr 13, 2021·Biomacromolecules·Ian W Hamley
Sep 22, 2020·Chembiochem : a European Journal of Chemical Biology·Zsofia Lengyel-ZhandIvan V Korendovych
Oct 3, 2020·Journal of Materials Chemistry. B, Materials for Biology and Medicine·Xia LiShuo Wang
Apr 25, 2020·Chembiochem : a European Journal of Chemical Biology·Liam R MarshallIvan V Korendovych
Jun 22, 2021·Chemical Communications : Chem Comm·Alexandra M Webster, Anna F A Peacock
Aug 25, 2020·Journal of the American Chemical Society·Michael S Wang, Michael H Hecht

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