Backbone resonance assignments of the Escherichia coli 62 kDa protein, Hsp31

J Kim, D Choi, C Park, KS Ryu - Biomolecular NMR Assignments, 2017 - Springer
Dimeric Hsp31 protein was first characterized as a holding chaperone of Escherichia coli (E.
coli), and has been suggested as having protease activity due to the presence of a potential …

[PDF][PDF] Per-deuteration and NMR experiments for the backbone assignment of 62 kDa protein, Hsp31

J Kim, D Choi, C Park, KS Ryu - Journal of the Korean Magnetic …, 2015 - academia.edu
Hsp31 protein is one of the members of DJ-1 superfamily proteins and has a dimeric
structure of which molecular weight (MW) is 62 kDa. The mutation of DJ-1 is closely related …