ArticleJournal of biomolecular NMR2011
A segmental labeling strategy for unambiguous determination of domain-domain interactions of large multi-domain proteins.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Semi-synthesis of labeled proteins for spectroscopic applications.Molecules (Basel, Switzerland) · 2013Review
- Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology.Journal of biomolecular NMR · 2013Article
- Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing.Journal of biomolecular NMR · 2012Article
- Topology of human apolipoprotein E3 uniquely regulates its diverse biological functions.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
NMR structural determination of large multi-domain proteins is a challenging task due to significant spectral overlap with a particular difficulty in unambiguous identification of domain-domain interactions. Segmental labeling is a NMR strategy that allows for isotopically labeling one domain and leaves the other domain unlabeled. This significantly simplifies spectral overlaps and allows for quick identification of domain-domain interaction. Here, a novel segmental labeling strategy is presented for detection of inter-domain NOEs. To identify domain-domain interactions in human apolipoprotein E (apoE), a multi-domain, 299-residues α-helical protein, on-column expressed protein ligation was utilized to generate a segmental-labeled apoE samples in which the N-terminal (NT-) domain was (2)H(99%)/(15)N-labeled whereas the C-terminal (CT-) domain was either (15)N- or (15)N/(13)C-labeled. 3-D (15)N-edited NOESY spectra of these segmental-labeled apoE samples allow for direct observation of the inter-domain NOEs between the backbone amide protons of the NT-domain and the aliphatic protons of the CT-domain. This straightforward approach permits unambiguous identification of 78 inter-domain NOEs, enabling accurate definition of the relative positions of both the NT- and the CT-domains and determination of the NMR structure of apoE.
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