Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide. / Oktaviani, Nur Alia; Risør, Michael W; Lee, Young-Ho; Megens, Rik P; de Jong, Djurre H; Otten, Renee; Scheek, Ruud M; Enghild, Jan J; Nielsen, Niels Christian; Ikegami, Takahisa; Mulder, Frans A A.

I: Journal of Biomolecular N M R, Bind 62, Nr. 2, 06.2015, s. 129-142.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Oktaviani, NA, Risør, MW, Lee, Y-H, Megens, RP, de Jong, DH, Otten, R, Scheek, RM, Enghild, JJ, Nielsen, NC, Ikegami, T & Mulder, FAA 2015, 'Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide', Journal of Biomolecular N M R, bind 62, nr. 2, s. 129-142. https://doi.org/10.1007/s10858-015-9925-8

APA

Oktaviani, N. A., Risør, M. W., Lee, Y-H., Megens, R. P., de Jong, D. H., Otten, R., ... Mulder, F. A. A. (2015). Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide. Journal of Biomolecular N M R, 62(2), 129-142. https://doi.org/10.1007/s10858-015-9925-8

CBE

Oktaviani NA, Risør MW, Lee Y-H, Megens RP, de Jong DH, Otten R, Scheek RM, Enghild JJ, Nielsen NC, Ikegami T, Mulder FAA. 2015. Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide. Journal of Biomolecular N M R. 62(2):129-142. https://doi.org/10.1007/s10858-015-9925-8

MLA

Vancouver

Oktaviani NA, Risør MW, Lee Y-H, Megens RP, de Jong DH, Otten R o.a. Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide. Journal of Biomolecular N M R. 2015 jun;62(2):129-142. https://doi.org/10.1007/s10858-015-9925-8

Author

Oktaviani, Nur Alia ; Risør, Michael W ; Lee, Young-Ho ; Megens, Rik P ; de Jong, Djurre H ; Otten, Renee ; Scheek, Ruud M ; Enghild, Jan J ; Nielsen, Niels Christian ; Ikegami, Takahisa ; Mulder, Frans A A. / Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide. I: Journal of Biomolecular N M R. 2015 ; Bind 62, Nr. 2. s. 129-142.

Bibtex

@article{f00f3cb4706d4e17b70a272fbff3b7b7,
title = "Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide",
abstract = "Co-solute paramagnetic relaxation enhancement (PRE) is an attractive way to speed up data acquisition in NMR spectroscopy by shortening the T 1 relaxation time of the nucleus of interest and thus the necessary recycle delay. Here, we present the rationale to utilize high-spin iron(III) as the optimal transition metal for this purpose and characterize the properties of its neutral chelate form Fe(DO3A) as a suitable PRE agent. Fe(DO3A) effectively reduces the T 1 values across the entire sequence of the intrinsically disordered protein α-synuclein with negligible impact on line width. The agent is better suited than currently used alternatives, shows no specific interaction with the polypeptide chain and, due to its high relaxivity, is effective at low concentrations and in 'proton-less' NMR experiments. By using Fe(DO3A) we were able to complete the backbone resonance assignment of a highly fibrillogenic peptide from α1-antitrypsin by acquiring the necessary suite of multidimensional NMR datasets in 3 h.",
author = "Oktaviani, {Nur Alia} and Ris{\o}r, {Michael W} and Young-Ho Lee and Megens, {Rik P} and {de Jong}, {Djurre H} and Renee Otten and Scheek, {Ruud M} and Enghild, {Jan J} and Nielsen, {Niels Christian} and Takahisa Ikegami and Mulder, {Frans A A}",
year = "2015",
month = "6",
doi = "10.1007/s10858-015-9925-8",
language = "English",
volume = "62",
pages = "129--142",
journal = "Journal of Biomolecular N M R",
issn = "0925-2738",
publisher = "Springer Netherlands",
number = "2",

}

RIS

TY - JOUR

T1 - Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide

AU - Oktaviani, Nur Alia

AU - Risør, Michael W

AU - Lee, Young-Ho

AU - Megens, Rik P

AU - de Jong, Djurre H

AU - Otten, Renee

AU - Scheek, Ruud M

AU - Enghild, Jan J

AU - Nielsen, Niels Christian

AU - Ikegami, Takahisa

AU - Mulder, Frans A A

PY - 2015/6

Y1 - 2015/6

N2 - Co-solute paramagnetic relaxation enhancement (PRE) is an attractive way to speed up data acquisition in NMR spectroscopy by shortening the T 1 relaxation time of the nucleus of interest and thus the necessary recycle delay. Here, we present the rationale to utilize high-spin iron(III) as the optimal transition metal for this purpose and characterize the properties of its neutral chelate form Fe(DO3A) as a suitable PRE agent. Fe(DO3A) effectively reduces the T 1 values across the entire sequence of the intrinsically disordered protein α-synuclein with negligible impact on line width. The agent is better suited than currently used alternatives, shows no specific interaction with the polypeptide chain and, due to its high relaxivity, is effective at low concentrations and in 'proton-less' NMR experiments. By using Fe(DO3A) we were able to complete the backbone resonance assignment of a highly fibrillogenic peptide from α1-antitrypsin by acquiring the necessary suite of multidimensional NMR datasets in 3 h.

AB - Co-solute paramagnetic relaxation enhancement (PRE) is an attractive way to speed up data acquisition in NMR spectroscopy by shortening the T 1 relaxation time of the nucleus of interest and thus the necessary recycle delay. Here, we present the rationale to utilize high-spin iron(III) as the optimal transition metal for this purpose and characterize the properties of its neutral chelate form Fe(DO3A) as a suitable PRE agent. Fe(DO3A) effectively reduces the T 1 values across the entire sequence of the intrinsically disordered protein α-synuclein with negligible impact on line width. The agent is better suited than currently used alternatives, shows no specific interaction with the polypeptide chain and, due to its high relaxivity, is effective at low concentrations and in 'proton-less' NMR experiments. By using Fe(DO3A) we were able to complete the backbone resonance assignment of a highly fibrillogenic peptide from α1-antitrypsin by acquiring the necessary suite of multidimensional NMR datasets in 3 h.

U2 - 10.1007/s10858-015-9925-8

DO - 10.1007/s10858-015-9925-8

M3 - Journal article

VL - 62

SP - 129

EP - 142

JO - Journal of Biomolecular N M R

JF - Journal of Biomolecular N M R

SN - 0925-2738

IS - 2

ER -