Electrochemical data on redox properties of human Cofilin-2 and its Mutant S3D

Electrochemical data on redox properties of human Cofilin-2 and its Mutant S3D

The reported data are related to a research paper entitled ''Phosphorylated cofilin-2 is more prone to oxidative modifications on Cys39 and favors amyloid fibril formation'' [1]. Info about the formation and redox properties of the disulfide bridge of a protein is quite difficult...

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Bibliographic Details
Main Authors: Marcello Pignataro, Giulia Di Rocco, Lidia Lancellotti, Fabrizio Bernini, Khaushik Subramanian, Elena Castellini, Carlo Augusto Bortolotti, Daniele Malferrari, Daniele Moro, Giovanni Valdrè, Marco Borsari, Federica del Monte
Format: Article
Language:English
Published: Elsevier 2020-12-01
Series:Data in Brief
Subjects:
Human cofilin
Disulfide bridge
Cyclic voltammetry
Redox properties
Electrochemistry
Cysteine
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340920312385

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http://www.sciencedirect.com/science/article/pii/S2352340920312385

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