1H, 13C and 15N resonance assignments of the bb′ domains of human protein disulfide isomerase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-07

AUTHORS

Alexey Yu. Denisov, Pekka Maattanen, Tara Sprules, David Y. Thomas, Kalle Gehring

ABSTRACT

Protein disulfide isomerase (PDI) participates in protein folding and catalyses formation of disulfide bonds. The b′ domain of human PDI contributes to binding unfolded proteins; its structure is stabilized by the b domain. Here, we report NMR chemical shift assignments for the bb′ fragment.

PAGES

129-130

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12104-007-9035-y

DOI

http://dx.doi.org/10.1007/s12104-007-9035-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017890413

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19636846


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