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...
| Autores principales: | , , , |
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| Formato: | Journal article |
| Lenguaje: | English |
| Publicado: |
Springer Nature
2021
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| _version_ | 1826300286273060864 |
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| author | Smith, LJ van Gunsteren, W Stankiewicz, B Hansen, N |
| author_facet | Smith, LJ van Gunsteren, W Stankiewicz, B Hansen, N |
| author_sort | Smith, LJ |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T05:14:51Z |
| format | Journal article |
| id | oxford-uuid:dcd38739-740f-499c-b33c-03e1f68e7ad5 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:14:51Z |
| publishDate | 2021 |
| publisher | Springer Nature |
| record_format | dspace |
| spelling | oxford-uuid:dcd38739-740f-499c-b33c-03e1f68e7ad52022-03-27T09:20:22ZOn the use of 3J-coupling NMR Data to derive structural information on proteinsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:dcd38739-740f-499c-b33c-03e1f68e7ad5EnglishSymplectic ElementsSpringer Nature2021Smith, LJvan Gunsteren, WStankiewicz, BHansen, NValues 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. |
| spellingShingle | Smith, LJ van Gunsteren, W Stankiewicz, B Hansen, N On the use of 3J-coupling NMR Data to derive structural information on proteins |
| title | On the use of 3J-coupling NMR Data to derive structural information on proteins |
| title_full | On the use of 3J-coupling NMR Data to derive structural information on proteins |
| title_fullStr | On the use of 3J-coupling NMR Data to derive structural information on proteins |
| title_full_unstemmed | On the use of 3J-coupling NMR Data to derive structural information on proteins |
| title_short | On the use of 3J-coupling NMR Data to derive structural information on proteins |
| title_sort | on the use of 3j coupling nmr data to derive structural information on proteins |
| work_keys_str_mv | AT smithlj ontheuseof3jcouplingnmrdatatoderivestructuralinformationonproteins AT vangunsterenw ontheuseof3jcouplingnmrdatatoderivestructuralinformationonproteins AT stankiewiczb ontheuseof3jcouplingnmrdatatoderivestructuralinformationonproteins AT hansenn ontheuseof3jcouplingnmrdatatoderivestructuralinformationonproteins |