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

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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 to early onset of Parkinson's disease. Hsp31 displays Zn+2-binding activity and was first reported to be a holding chaperone in E. coli. Its additional glyoxalase III active has recently been characterized. Moreover, an incubation at 60 degrees C induces Hsp31 protein to form a high MW oligomer (HMW) in vitro, which accomplishes an elevated holding chaperone activity. The NMR technique is elegant method to probe any local or global structural change of a protein in responses to environmental stresses (heat, pH, and metal). Although the presence of the backbone chemical shifts (bbCSs) is a prerequisite for detailed NMR analyses of the structural changes, general HSQC-based triple resonance experiments could not be used for 62 kDa Hsp31 protein. Here, we prepared the per-deuterated Hsp31 and performed the TROSY-based triple resonance experiments for the bbCSs assignment. Here, detailed processes of per-deuteration and the NMR experiments are described for other similar NMR approaches.
Publisher
KOREAN MAGNETIC RESONANCE SOC
Issue Date
2015-12
Language
English
Article Type
Article
Citation

JOURNAL OF THE KOREAN MAGNETIC RESONANCE SOCIETY, v.19, no.3, pp.112 - 118

ISSN
1226-6531
DOI
10.6564/JKMRS.2015.19.3.112
URI
http://hdl.handle.net/10203/261662
Appears in Collection
BS-Journal Papers(저널논문)
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