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

Research output: Contribution to journal › Article › 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.

Original language	English
Pages (from-to)	253-261
Number of pages	9
Journal	Journal of Biomolecular NMR
Volume	62
Issue number	3
DOIs	https://doi.org/10.1007/s10858-015-9956-1
Publication status	Published - Jul 2015
Externally published	Yes

Keywords

Automation
Magic-angle spinning
Protein resonance assignment
Proton detection

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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",

}

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, no. 3, pp. 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

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