Protein residue linking in a single spectrum for magic-angle spinning NMR assignment

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00084849" target="_blank" >RIV/00216224:14740/15:00084849 - isvavai.cz</a>

Výsledek na webu

<a href="http://download.springer.com/static/pdf/256/art%253A10.1007%252Fs10858-015-9956-1.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs10858-015-9956-1&token2=exp=1448368928~acl=%2Fstatic%2Fpdf%2F256%2Fart%25253A10.1007%25252Fs10858-015-99" target="_blank" >http://download.springer.com/static/pdf/256/art%253A10.1007%252Fs10858-015-9956-1.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs10858-015-9956-1&token2=exp=1448368928~acl=%2Fstatic%2Fpdf%2F256%2Fart%25253A10.1007%25252Fs10858-015-99</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10858-015-9956-1" target="_blank" >10.1007/s10858-015-9956-1</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Protein residue linking in a single spectrum for magic-angle spinning NMR assignment

Popis výsledku v původním jazyce

Here we introduce a new pulse sequence for resonance assignment that halves the number of data sets required for sequential linking by directly correlating sequential amide resonances in a single diagonal-free spectrum. The method is demonstrated with both microcrystalline and sedimented deuterated proteins spinning at 60 and 111 kHz, and a fully protonated microcrystalline protein spinning at 111 kHz, with as little as 0.5 mg protein sample. We find that amide signals have a low chance of ambiguous linkage, which is further improved by linking in both forward and backward directions. The spectra obtained are amenable to automated resonance assignment using general-purpose software such as UNIO-MATCH.

Název v anglickém jazyce

Protein residue linking in a single spectrum for magic-angle spinning NMR assignment

Popis výsledku anglicky

Here we introduce a new pulse sequence for resonance assignment that halves the number of data sets required for sequential linking by directly correlating sequential amide resonances in a single diagonal-free spectrum. The method is demonstrated with both microcrystalline and sedimented deuterated proteins spinning at 60 and 111 kHz, and a fully protonated microcrystalline protein spinning at 111 kHz, with as little as 0.5 mg protein sample. We find that amide signals have a low chance of ambiguous linkage, which is further improved by linking in both forward and backward directions. The spectra obtained are amenable to automated resonance assignment using general-purpose software such as UNIO-MATCH.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

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

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Svazek periodika

62

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

253-261

Kód UT WoS článku

000357489200003

EID výsledku v databázi Scopus

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