Turncoat Polypeptides: We Adapt to Our Environment
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 prot...
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Veröffentlicht in: | Chembiochem : a European journal of chemical biology 2020-02, Vol.21 (4), p.432-441 |
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Sprache: | eng |
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Zusammenfassung: | 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.
Blending into the surroundings: A common interpretation of Anfinsen's hypothesis is that one amino acid sequence folds into a single, native, ordered state that, in turn, is responsible for the function of the protein. However, turncoat polypeptides are sequences that can switch between different structural states upon variation in the surrounding conditions or under the effect of trigger agents. |
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ISSN: | 1439-4227 1439-7633 |
DOI: | 10.1002/cbic.201900446 |