A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
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-tekijät tai -toimittajat


Julkaisun tiedot

Julkaisun kaikki tekijät tai toimittajatTossavainen, Helena; Salovaara, Santeri; Hellman, Maarit; Ihalin, Riikka; Permi, Perttu

Lehti tai sarjaJournal of Biomolecular NMR

ISSN0925-2738

eISSN1573-5001

Julkaisuvuosi2020

Volyymi74

Lehden numero2-3

Artikkelin sivunumerot147-159

KustantajaSpringer

JulkaisumaaAlankomaat

Julkaisun kielienglanti

DOIhttps://doi.org/10.1007/s10858-020-00299-w

Julkaisun avoin saatavuusAvoimesti saatavilla

Julkaisukanavan avoin saatavuusOsittain avoin julkaisukanava

Julkaisu on rinnakkaistallennettu (JYX)https://jyx.jyu.fi/handle/123456789/68258


Tiivistelmä

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.


YSO-asiasanatproteiinitbakteeritresonanssiNMR-spektroskopia

Vapaat asiasanatAggregatibacter actinomycetemcomitans; BilRI; IDP; intrinsically disordered protein; resonance assignment


Liittyvät organisaatiot


Hankkeet, joissa julkaisu on tehty


OKM-raportointiKyllä

Raportointivuosi2020

JUFO-taso1


Viimeisin päivitys 2024-03-04 klo 21:16