High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.
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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, Vol. 3, No. 6, 6, 2008, p. 2359.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -