Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00114136" target="_blank" >RIV/00216224:14740/20:00114136 - isvavai.cz</a>

Výsledek na webu

<a href="https://link.springer.com/article/10.1007%2Fs10858-019-00298-6" target="_blank" >https://link.springer.com/article/10.1007%2Fs10858-019-00298-6</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10858-019-00298-6" target="_blank" >10.1007/s10858-019-00298-6</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR

Popis výsledku v původním jazyce

Improving our understanding of nanosecond motions in disordered proteins requires the enhanced sampling of the spectral density function obtained from relaxation at low magnetic fields. High-resolution relaxometry and two-field NMR measurements of relaxation have, so far, only been based on the recording of one- or two-dimensional spectra, which provide insufficient resolution for challenging disordered proteins. Here, we introduce a 3D-HNCO-based two-field NMR experiment for measurements of protein backbone 15Namide longitudinal relaxation rates. The experiment provides accurate longitudinal relaxation rates at low field (0.33 T in our case) preserving the resolution and sensitivity typical for high-field NMR spectroscopy. Radiofrequency pulses applied on six different radiofrequency channels are used to manipulate the spin system at both fields. The experiment was demonstrated on the C-terminal domain of delta subunit of RNA polymerase from Bacillus subtilis, a protein with highly repetitive amino-acid sequence and very low dispersion of backbone chemical shifts.

Název v anglickém jazyce

Boosting the resolution of low-field 15N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR

Popis výsledku anglicky

Improving our understanding of nanosecond motions in disordered proteins requires the enhanced sampling of the spectral density function obtained from relaxation at low magnetic fields. High-resolution relaxometry and two-field NMR measurements of relaxation have, so far, only been based on the recording of one- or two-dimensional spectra, which provide insufficient resolution for challenging disordered proteins. Here, we introduce a 3D-HNCO-based two-field NMR experiment for measurements of protein backbone 15Namide longitudinal relaxation rates. The experiment provides accurate longitudinal relaxation rates at low field (0.33 T in our case) preserving the resolution and sensitivity typical for high-field NMR spectroscopy. Radiofrequency pulses applied on six different radiofrequency channels are used to manipulate the spin system at both fields. The experiment was demonstrated on the C-terminal domain of delta subunit of RNA polymerase from Bacillus subtilis, a protein with highly repetitive amino-acid sequence and very low dispersion of backbone chemical shifts.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GJ18-04197Y" target="_blank" >GJ18-04197Y: Charakterizace flexibilních oblastí RNA polymerázy Bacillus subtilis</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of biomolecular NMR

ISSN

0925-2738

e-ISSN

—

Svazek periodika

74

Číslo periodika v rámci svazku

2-3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

139-145

Kód UT WoS článku

000520461300004

EID výsledku v databázi Scopus

2-s2.0-85078226018