On the use of 3J-coupling NMR Data to derive structural information on proteins
Values of 3 J-couplings as obtained from NMR experiments on proteins cannot easily be used to determine protein structure due to the difficulty of accounting for the high sensitivity of intermediate 3 J-coupling values (4 – 8 Hz) to the averaging period that must cover the conformational variability...
| Main Authors: | , , , |
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| פורמט: | Journal article |
| שפה: | English |
| יצא לאור: |
Springer Nature
2021
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| סיכום: | Values of 3
J-couplings as obtained from NMR experiments on proteins cannot
easily be used to determine protein structure due to the difficulty of accounting for the
high sensitivity of intermediate 3
J-coupling values (4 – 8 Hz) to the averaging period
that must cover the conformational variability of the torsional angle related to the 3
Jcoupling, and due to the difficulty of handling the multiple-valued character of the
inverse Karplus relation between torsional angle and 3
J-coupling. Both problems can
be solved by using 3
J-coupling time-averaging local-elevation restraining MD
simulation. Application to the protein hen egg white lysozyme using 213 backbone and
side-chain 3
J-coupling restraints shows that a conformational ensemble compatible
with the experimental data can be obtained using this technique, and that accounting
for averaging and the ability of the algorithm to escape from local minima for the
torsional angle induced by the Karplus relation, are essential for a comprehensive use
of 3
J-coupling data in protein structure determination. |
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