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Turncoat Polypeptides: We Adapt to Our Environment
Author(s) -
ZamoraCarreras Héctor,
Maestro Beatriz,
Sanz Jesús M.,
Jiménez M. Angeles
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900446
Subject(s) - computational biology , folding (dsp implementation) , protein folding , function (biology) , sequence (biology) , biomedicine , peptide sequence , biology , biochemistry , chemistry , bioinformatics , genetics , engineering , gene , electrical engineering
Abstract A common interpretation of Anfinsen's hypothesis states that one amino acid sequence should fold into a single, native, ordered state, or a highly similar set thereof, coinciding with the global minimum in the folding‐energy landscape, which, in turn, is responsible for the function of the protein. However, this classical view is challenged by many proteins and peptide sequences, which can adopt exchangeable, significantly dissimilar conformations that even fulfill different biological roles. The similarities and differences of concepts related to these proteins, mainly chameleon sequences, metamorphic proteins, and switch peptides, which are all denoted herein “turncoat” polypeptides, are reviewed. As well as adding a twist to the conventional view of protein folding, the lack of structural definition adds clear versatility to the activity of proteins and can be used as a tool for protein design and further application in biotechnology and biomedicine.