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


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

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Ministry reporting: Yes

Reporting Year: 2020

JUFO rating: 1

Last updated on 2022-14-09 at 11:57