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High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.

Standard

High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy. / Korukottu, Jegannath; Schneider, Robert; Vijayan, Vinesh; Lange, Adam; Pongs, Olaf; Becker, Stefan; Baldus, Marc; Zweckstetter, Markus.

in: PLOS ONE, Jahrgang 3, Nr. 6, 6, 2008, S. 2359.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Korukottu, J, Schneider, R, Vijayan, V, Lange, A, Pongs, O, Becker, S, Baldus, M & Zweckstetter, M 2008, 'High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.', PLOS ONE, Jg. 3, Nr. 6, 6, S. 2359. https://doi.org/10.1371/journal.pone.0002359

APA

Korukottu, J., Schneider, R., Vijayan, V., Lange, A., Pongs, O., Becker, S., Baldus, M., & Zweckstetter, M. (2008). High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy. PLOS ONE, 3(6), 2359. [6]. https://doi.org/10.1371/journal.pone.0002359

Vancouver

Korukottu J, Schneider R, Vijayan V, Lange A, Pongs O, Becker S et al. High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy. PLOS ONE. 2008;3(6):2359. 6. https://doi.org/10.1371/journal.pone.0002359

Bibtex

@article{39deda385ddc4be6b836d89d18140b71,
title = "High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.",
abstract = "High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.",
author = "Jegannath Korukottu and Robert Schneider and Vinesh Vijayan and Adam Lange and Olaf Pongs and Stefan Becker and Marc Baldus and Markus Zweckstetter",
year = "2008",
doi = "10.1371/journal.pone.0002359",
language = "Deutsch",
volume = "3",
pages = "2359",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "6",

}

RIS

TY - JOUR

T1 - High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.

AU - Korukottu, Jegannath

AU - Schneider, Robert

AU - Vijayan, Vinesh

AU - Lange, Adam

AU - Pongs, Olaf

AU - Becker, Stefan

AU - Baldus, Marc

AU - Zweckstetter, Markus

PY - 2008

Y1 - 2008

N2 - High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.

AB - High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.

U2 - 10.1371/journal.pone.0002359

DO - 10.1371/journal.pone.0002359

M3 - SCORING: Zeitschriftenaufsatz

VL - 3

SP - 2359

JO - PLOS ONE

JF - PLOS ONE

SN - 1932-6203

IS - 6

M1 - 6

ER -