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Turncoat Polypeptides: we adapt to our environment

AuthorsZamora-Carreras, H.; Maestro, Beatriz; Sanz, Jesús M. ; Jiménez, M. Angeles
KeywordsChameleon sequences
Metamorphic proteins
Protein folding
Protein structures
Switch peptides
Issue Date28-Aug-2019
CitationChemBioChem 21: 432–441 (2020)
AbstractAcommon interpretation of Anfinsen’s hypothesisstates thatone amino acid sequence should fold into asingle, native, or-dered state, or ahighly similarset thereof,coinciding with theglobal minimum in the folding- energy landscape, which,inturn, is responsible for the functionofthe protein. However,this classical view is challenged by many proteins and peptidesequences, which can adopt exchangeable, significantly dissim-ilar conformations that even fulfill different biological roles.The simila rities and differences of co ncepts related to theseproteins,mainly chameleon sequences,metamorphic proteins,and switch peptides, whichare all denoted herein “turncoat”polypeptides, are review ed. As well as adding atwist to theconventional view of protein folding, the lack of structural defi-nition adds clear versatility to the activity of proteins and canbe used as atool for protein design and further applicationinbiotechnology and biomedicine.
Description10 pags., 4 figs.
Publisher version (URL)https://doi.org/10.1002/cbic.201900446
Appears in Collections:(IQFR) Artículos
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