A1 Journal article (refereed)
Dispersion from Cα or NH : 4D experiments for backbone resonance assignment of intrinsically disordered proteins (2020)
Tossavainen, H., Salovaara, S., Hellman, M., Ihalin, R., & Permi, P. (2020). Dispersion from Cα or NH : 4D experiments for backbone resonance assignment of intrinsically disordered proteins. Journal of Biomolecular NMR, 74(2-3), 147-159. https://doi.org/10.1007/s10858-020-00299-w
JYU authors or editors
Publication details
All authors or editors: Tossavainen, Helena; Salovaara, Santeri; Hellman, Maarit; Ihalin, Riikka; Permi, Perttu
Journal or series: Journal of Biomolecular NMR
ISSN: 0925-2738
eISSN: 1573-5001
Publication year: 2020
Volume: 74
Issue number: 2-3
Pages range: 147-159
Publisher: Springer
Publication country: Netherlands
Publication language: English
DOI: https://doi.org/10.1007/s10858-020-00299-w
Publication open access: Openly available
Publication channel open access: Partially open access channel
Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/68258
Abstract
Resonance assignment of intrinsically disordered proteins is remarkably challenging due to scant chemical shift dispersion arising from conformational heterogeneity. The challenge is even greater if repeating segments are present in the amino acid sequence. To forward unambiguous resonance assignment of intrinsically disordered proteins, we present iHACANCO, HACACON and (HACA)CONCAHA, three Hα-detected 4D experiments with Cα as an additional dimension. In addition, we present (HACA)CON(CA)NH and (HACA)N(CA)CONH, new 4D Hα-start, HN-detect experiments which have two NH dimensions to enhance peak dispersion in a sequential walk through C', NH and HN, and provide more accurate NH/HN chemical shifts than those that can be obtained from a crowded 1H, 15N-HSQC spectrum. Application of these 4D experiments is demonstrated using BilRI (165 aa), an outer-membrane intrinsically disordered protein from the opportunistic oral pathogen Aggregatibacter actinomycetemcomitans. BilRI amino acid sequence encompasses three very similar repeats with a 13-residue identical stretch in two of them.
Keywords: proteins; bacteria; resonance; NMR spectroscopy
Free keywords: Aggregatibacter actinomycetemcomitans; BilRI; IDP; intrinsically disordered protein; resonance assignment
Contributing organizations
Related projects
- Conformational properties of intrinsically disordered proteins - biophysical characterization
- Permi, Perttu
- Research Council of Finland
Ministry reporting: Yes
VIRTA submission year: 2020
JUFO rating: 1