The making of a protein is based on the combination of 20 different monomers (22 considering selenocysteine and pyrrolysine, the latest present only in some archaea and bacteria) giving the possibility of building a variety of structures from the simplest to the most complex, rigid or highly dynamic, and suited to carry out a wide range of structural and functional roles [...].

Editorial of special issue “protein post-translational modifications in signal transduction and diseases”

D'amore C.
;
Salvi M.
2021

Abstract

The making of a protein is based on the combination of 20 different monomers (22 considering selenocysteine and pyrrolysine, the latest present only in some archaea and bacteria) giving the possibility of building a variety of structures from the simplest to the most complex, rigid or highly dynamic, and suited to carry out a wide range of structural and functional roles [...].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/3387761
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