| ANDREAS, Loren B., Jan STANĚK, Tanguy LE MARCHAND, Andrea BERTARELLO, Diane Cala-De PAEPE, Daniela LALLI, Magdaléna KREJČÍKOVÁ, Camille DOYEN, Carl OSTER, Benno KNOTT, Sebastian WEGNER, Frank ENGELKE, Isabella C. FELLI, Roberta PIERATTELLI, Nicholas E. DIXON, Lyndon EMSLEY, Torsten HERRMANN and Guido PINTACUDA. Protein residue linking in a single spectrum for magic-angle spinning NMR assignment. Journal of biomolecular NMR. Dordrecht: Springer, 2015, vol. 62, No 3, p. 253-261. ISSN 0925-2738. Available from: https://dx.doi.org/10.1007/s10858-015-9956-1. |
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@article{1318520,
author = {Andreas, Loren B. and Staněk, Jan and Le Marchand, Tanguy and Bertarello, Andrea and Paepe, Diane CalaandDe and Lalli, Daniela and Krejčíková, Magdaléna and Doyen, Camille and Oster, Carl and Knott, Benno and Wegner, Sebastian and Engelke, Frank and Felli, Isabella C. and Pierattelli, Roberta and Dixon, Nicholas E. and Emsley, Lyndon and Herrmann, Torsten and Pintacuda, Guido},
article_location = {Dordrecht},
article_number = {3},
doi = {http://dx.doi.org/10.1007/s10858-015-9956-1},
keywords = {Magic-angle spinning; Protein resonance assignment; Proton detection; Automation},
language = {eng},
issn = {0925-2738},
journal = {Journal of biomolecular NMR},
title = {Protein residue linking in a single spectrum for magic-angle spinning NMR assignment},
url = {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},
volume = {62},
year = {2015}
}
TY - JOUR
ID - 1318520
AU - Andreas, Loren B. - Staněk, Jan - Le Marchand, Tanguy - Bertarello, Andrea - Paepe, Diane Cala-De - Lalli, Daniela - Krejčíková, Magdaléna - Doyen, Camille - Oster, Carl - Knott, Benno - Wegner, Sebastian - Engelke, Frank - Felli, Isabella C. - Pierattelli, Roberta - Dixon, Nicholas E. - Emsley, Lyndon - Herrmann, Torsten - Pintacuda, Guido
PY - 2015
TI - Protein residue linking in a single spectrum for magic-angle spinning NMR assignment
JF - Journal of biomolecular NMR
VL - 62
IS - 3
SP - 253-261
EP - 253-261
PB - Springer
SN - 09252738
KW - Magic-angle spinning
KW - Protein resonance assignment
KW - Proton detection
KW - Automation
UR - 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
L2 - 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
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.
ER -
ANDREAS, Loren B., Jan STANĚK, Tanguy LE MARCHAND, Andrea BERTARELLO, Diane Cala-De PAEPE, Daniela LALLI, Magdaléna KREJČÍKOVÁ, Camille DOYEN, Carl OSTER, Benno KNOTT, Sebastian WEGNER, Frank ENGELKE, Isabella C. FELLI, Roberta PIERATTELLI, Nicholas E. DIXON, Lyndon EMSLEY, Torsten HERRMANN and Guido PINTACUDA. Protein residue linking in a single spectrum for magic-angle spinning NMR assignment. \textit{Journal of biomolecular NMR}. Dordrecht: Springer, 2015, vol.~62, No~3, p.~253-261. ISSN~0925-2738. Available from: https://dx.doi.org/10.1007/s10858-015-9956-1.
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