Probing short and long-range interactions in native collagen inside the bone matrix by BioSolids CryoProbe
© 2020 John Wiley & Sons, Ltd.
Veröffentlicht in: | Magnetic resonance in chemistry : MRC. - 1985. - 59(2021), 2 vom: 20. Feb., Seite 99-107 |
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1. Verfasser: | |
Weitere Verfasser: | , , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2021
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Zugriff auf das übergeordnete Werk: | Magnetic resonance in chemistry : MRC |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't CryoProbe bone collagen magic angle spinning solid-state NMR Carbon Isotopes Nitrogen Isotopes Nitrogen-15 mehr... |
Zusammenfassung: | © 2020 John Wiley & Sons, Ltd. Solid-state nuclear magnetic resonance is a promising technique to probe bone mineralization and interaction of collagen protein in the native state. However, many of the developments are hampered due to the low sensitivity of the technique. In this article, we report solid-state nuclear magnetic resonance (NMR) experiments using the newly developed BioSolids CryoProbe™ to access its applicability for elucidating the atomic-level structural details of collagen protein in native state inside the bone. We report here approximately a fourfold sensitivity enhancement in the natural abundance 13 C spectrum compared with the room temperature conventional solid-state NMR probe. With the advantage of sensitivity enhancement, we have been able to perform natural abundance 15 N cross-polarization magic angle spinning (CPMAS) and two-dimensional (2D) 1 H-13 C heteronuclear correlation (HETCOR) experiments of native collagen within a reasonable timeframe. Due to high sensitivity, 2D 1 H/13 C HETCOR experiments have helped in detecting several short and long-range interactions of native collagen assembly, thus significantly expanding the scope of the method to such challenging biomaterials |
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Beschreibung: | Date Completed 19.07.2021 Date Revised 19.07.2021 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1097-458X |
DOI: | 10.1002/mrc.5084 |