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Complete sequential assignment and secondary structure prediction of the cannulae forming protein CanA from the hyperthermophilic archaeon Pyrodictium abyssi

URN to cite this document:
urn:nbn:de:bvb:355-epub-447210
DOI to cite this document:
10.5283/epub.44721
Kalbitzer, Hans Robert ; Kreitner, Raphael ; Munte, Claudia E. ; Singer, Katrin ; Stetter, Karl Otto ; Horn, Gudrun ; Kremer, Werner
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License: Creative Commons Attribution 4.0
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Date of publication of this fulltext: 05 Feb 2021 08:53

This publication is part of the DEAL contract with Springer.


Abstract

CanA from Pyrodictium abyssi forms a heat-resistant organic hollow-fiber network together with CanB and CanC. An N-terminally truncated construct of CanA (K-1-CanA) gave NMR spectra of good quality that could be assigned by three-dimensional NMR methods on N-15 and C-13-N-15 enriched protein. We assigned the chemical shifts of 96% of all backbone H-1(N) atoms, 98% of all backbone N-15 atoms, 100% ...

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