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

Loren B. Andreas; Jan Stanek; Tanguy Le Marchand; Andrea Bertarello; Diane Cala-De Paepe; Daniela Lalli; Magdaléna Krejčíková; Camille Doyen; Carl Öster; Benno Knott; Sebastian Wegner; Frank Engelke; Isabella C. Felli; Roberta Pierattelli; Nicholas E. Dixon; Lyndon Emsley; Torsten Herrmann; Guido Pintacuda

doi:10.1007/s10858-015-9956-1

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

Loren B. Andreas, Jan Stanek, Tanguy Le Marchand, Andrea Bertarello, Diane Cala-De Paepe, Daniela Lalli, Magdaléna Krejčíková, Camille Doyen, Carl Öster, Benno Knott, Sebastian Wegner, Frank Engelke, Isabella C. Felli, Roberta Pierattelli, Nicholas E. Dixon, Lyndon Emsley, Torsten Herrmann, Guido Pintacuda

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

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.

Lingua originale	Inglese
pagine (da-a)	253-261
Numero di pagine	9
Rivista	Journal of Biomolecular NMR
Volume	62
Numero di pubblicazione	3
DOI	https://doi.org/10.1007/s10858-015-9956-1
Stato di pubblicazione	Pubblicato - lug 2015
Pubblicato esternamente	Sì

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10.1007/s10858-015-9956-1

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Andreas, L. B., Stanek, J., Le Marchand, T., Bertarello, A., Cala-De Paepe, D., Lalli, D., Krejčíková, M., Doyen, C., Öster, C., Knott, B., Wegner, S., Engelke, F., Felli, I. C., Pierattelli, R., Dixon, N. E., Emsley, L., Herrmann, T., & Pintacuda, G. (2015). Protein residue linking in a single spectrum for magic-angle spinning NMR assignment. Journal of Biomolecular NMR, 62(3), 253-261. https://doi.org/10.1007/s10858-015-9956-1

@article{ce8a3fe5843f417caaef6c8b68241b7f,

title = "Protein residue linking in a single spectrum for magic-angle spinning NMR assignment",

abstract = "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.",

keywords = "Automation, Magic-angle spinning, Protein resonance assignment, Proton detection",

author = "Andreas, {Loren B.} and Jan Stanek and {Le Marchand}, Tanguy and Andrea Bertarello and {Cala-De Paepe}, Diane and Daniela Lalli and Magdal{\'e}na Krej{\v c}{\'i}kov{\'a} and Camille Doyen and Carl {\"O}ster and Benno Knott and Sebastian Wegner and Frank Engelke and Felli, {Isabella C.} and Roberta Pierattelli and Dixon, {Nicholas E.} and Lyndon Emsley and Torsten Herrmann and Guido Pintacuda",

note = "Publisher Copyright: {\textcopyright} Springer Science+Business Media Dordrecht 2015.",

year = "2015",

month = jul,

doi = "10.1007/s10858-015-9956-1",

language = "English",

volume = "62",

pages = "253--261",

journal = "Journal of Biomolecular NMR",

issn = "0925-2738",

publisher = "Springer Science and Business Media B.V.",

number = "3",

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Andreas, LB, Stanek, J, Le Marchand, T, Bertarello, A, Cala-De Paepe, D, Lalli, D, Krejčíková, M, Doyen, C, Öster, C, Knott, B, Wegner, S, Engelke, F, Felli, IC, Pierattelli, R, Dixon, NE, Emsley, L, Herrmann, T & Pintacuda, G 2015, 'Protein residue linking in a single spectrum for magic-angle spinning NMR assignment', Journal of Biomolecular NMR, vol. 62, n. 3, pagg. 253-261. https://doi.org/10.1007/s10858-015-9956-1

TY - JOUR

T1 - Protein residue linking in a single spectrum for magic-angle spinning NMR assignment

AU - Andreas, Loren B.

AU - Stanek, Jan

AU - Le Marchand, Tanguy

AU - Bertarello, Andrea

AU - Cala-De Paepe, Diane

AU - Lalli, Daniela

AU - Krejčíková, Magdaléna

AU - Doyen, Camille

AU - Öster, Carl

AU - Knott, Benno

AU - Wegner, Sebastian

AU - Engelke, Frank

AU - Felli, Isabella C.

AU - Pierattelli, Roberta

AU - Dixon, Nicholas E.

AU - Emsley, Lyndon

AU - Herrmann, Torsten

AU - Pintacuda, Guido

PY - 2015/7

Y1 - 2015/7

N2 - 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.

AB - 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.

KW - Automation

KW - Magic-angle spinning

KW - Protein resonance assignment

KW - Proton detection

UR - http://www.scopus.com/inward/record.url?scp=84944441197&partnerID=8YFLogxK

U2 - 10.1007/s10858-015-9956-1

DO - 10.1007/s10858-015-9956-1

M3 - Article

SN - 0925-2738

VL - 62

SP - 253

EP - 261

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

IS - 3

ER -

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

Abstract

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