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Probing short and long‐range interactions in native collagen inside the bone matrix by BioSolids CryoProbe
Author(s) -
Tiwari Nidhi,
Wegner Sebastian,
Hassan Alia,
Dwivedi Navneet,
Rai RamaNand,
Sinha Neeraj
Publication year - 2021
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.5084
Subject(s) - chemistry , heteronuclear molecule , solid state nuclear magnetic resonance , magic angle spinning , nuclear magnetic resonance , biosolids , nuclear magnetic resonance spectroscopy , stereochemistry , physics , engineering , environmental engineering
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.