ArticleBiomolecular NMR assignments2011
1H, 13C, and 15N NMR assignments of the Pyrococcus abyssi DNA polymerase II intein.
Article in Biomolecular NMR assignments, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 4 citations in OpenAlex.
- Allosteric Influence of Extremophile Hairpin Motif Mutations on the Protein Splicing Activity of a Hyperthermophilic Intein.Biochemistry · 2020Article
- Intramolecular disulfide bond between catalytic cysteines in an intein precursor.Journal of the American Chemical Society · 2012Article
- Structural and mutational studies of a hyperthermophilic intein from DNA polymerase II of Pyrococcus abyssi.The Journal of biological chemistry · 2011Article
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6 authors at 2 institutions in 1 country.
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Abstract
Protein splicing is a precise post-translational process mediated by inteins. Inteins are intervening proteins that cleave themselves from a precursor protein while joining the flanking sequences. Here we report the (15)N, (13)C, and (1)H chemical shift assignments of the intein from DNA polymerase II of Pyrococcus abyssi (Pab PolII intein), which has been recombinantly overexpressed and isotopically labeled. The NMR assignments of Pab PolII intein are essential for solution structure determination and protein dynamics study.
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