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 [...].File in questo prodotto:
File | Dimensione | Formato | |
---|---|---|---|
ijms-22-02232-v2.pdf
accesso aperto
Tipologia:
Published (Publisher's Version of Record)
Licenza:
Creative commons
Dimensione
194.21 kB
Formato
Adobe PDF
|
194.21 kB | Adobe PDF | Visualizza/Apri |
Pubblicazioni consigliate
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.