The Experts below are selected from a list of 360 Experts worldwide ranked by ideXlab platform
Ayyalusamy Ramamoorthy - One of the best experts on this subject based on the ideXlab platform.
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
Journal of Physical Chemistry B, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the 1H intrinsic spin–lattice (T1) relaxation times measured in natural-abundance 13C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state 13C CPMAS experiments were conducted on ...
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
The Journal of Physical Chemistry, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the ¹H intrinsic spin–lattice (T₁) relaxation times measured in natural-abundance ¹³C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state ¹³C CPMAS experiments were conducted on type I collagen (bovine tendon), bovine cortical bone, and demineralized bovine cortical bone, each in powdered form, to measure the ¹H T₁ values in the absence and in the presence of 30 mM Cu(II)(NH₄)₂EDTA. Our results show that the ¹H T₁ values were successfully reduced by a factor of 2.2, 2.9, and 3.2 for bovine cortical bone, type I collagen, and demineralized bone, respectively, without reducing the spectral resolution and thus enabling faster data acquisition. In addition, paramagnetic quenching of particular ¹³C NMR resonances on exposure to Cu²⁺ ions in the absence of mineral was also observed, potentially suggesting the relative proximity of three main amino acids in the protein backbone (glycine, proline, and alanine) to the bone mineral surface.
Kamal H Mroue - One of the best experts on this subject based on the ideXlab platform.
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
Journal of Physical Chemistry B, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the 1H intrinsic spin–lattice (T1) relaxation times measured in natural-abundance 13C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state 13C CPMAS experiments were conducted on ...
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
The Journal of Physical Chemistry, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the ¹H intrinsic spin–lattice (T₁) relaxation times measured in natural-abundance ¹³C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state ¹³C CPMAS experiments were conducted on type I collagen (bovine tendon), bovine cortical bone, and demineralized bovine cortical bone, each in powdered form, to measure the ¹H T₁ values in the absence and in the presence of 30 mM Cu(II)(NH₄)₂EDTA. Our results show that the ¹H T₁ values were successfully reduced by a factor of 2.2, 2.9, and 3.2 for bovine cortical bone, type I collagen, and demineralized bone, respectively, without reducing the spectral resolution and thus enabling faster data acquisition. In addition, paramagnetic quenching of particular ¹³C NMR resonances on exposure to Cu²⁺ ions in the absence of mineral was also observed, potentially suggesting the relative proximity of three main amino acids in the protein backbone (glycine, proline, and alanine) to the bone mineral surface.
Neil Mackinnon - One of the best experts on this subject based on the ideXlab platform.
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
Journal of Physical Chemistry B, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the 1H intrinsic spin–lattice (T1) relaxation times measured in natural-abundance 13C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state 13C CPMAS experiments were conducted on ...
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
The Journal of Physical Chemistry, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the ¹H intrinsic spin–lattice (T₁) relaxation times measured in natural-abundance ¹³C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state ¹³C CPMAS experiments were conducted on type I collagen (bovine tendon), bovine cortical bone, and demineralized bovine cortical bone, each in powdered form, to measure the ¹H T₁ values in the absence and in the presence of 30 mM Cu(II)(NH₄)₂EDTA. Our results show that the ¹H T₁ values were successfully reduced by a factor of 2.2, 2.9, and 3.2 for bovine cortical bone, type I collagen, and demineralized bone, respectively, without reducing the spectral resolution and thus enabling faster data acquisition. In addition, paramagnetic quenching of particular ¹³C NMR resonances on exposure to Cu²⁺ ions in the absence of mineral was also observed, potentially suggesting the relative proximity of three main amino acids in the protein backbone (glycine, proline, and alanine) to the bone mineral surface.
Michael D Morris - One of the best experts on this subject based on the ideXlab platform.
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
Journal of Physical Chemistry B, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the 1H intrinsic spin–lattice (T1) relaxation times measured in natural-abundance 13C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state 13C CPMAS experiments were conducted on ...
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
The Journal of Physical Chemistry, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the ¹H intrinsic spin–lattice (T₁) relaxation times measured in natural-abundance ¹³C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state ¹³C CPMAS experiments were conducted on type I collagen (bovine tendon), bovine cortical bone, and demineralized bovine cortical bone, each in powdered form, to measure the ¹H T₁ values in the absence and in the presence of 30 mM Cu(II)(NH₄)₂EDTA. Our results show that the ¹H T₁ values were successfully reduced by a factor of 2.2, 2.9, and 3.2 for bovine cortical bone, type I collagen, and demineralized bone, respectively, without reducing the spectral resolution and thus enabling faster data acquisition. In addition, paramagnetic quenching of particular ¹³C NMR resonances on exposure to Cu²⁺ ions in the absence of mineral was also observed, potentially suggesting the relative proximity of three main amino acids in the protein backbone (glycine, proline, and alanine) to the bone mineral surface.
David H Kohn - One of the best experts on this subject based on the ideXlab platform.
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
Journal of Physical Chemistry B, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the 1H intrinsic spin–lattice (T1) relaxation times measured in natural-abundance 13C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state 13C CPMAS experiments were conducted on ...
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high resolution structural insights into bone a solid state nmr relaxation study utilizing paramagnetic doping
The Journal of Physical Chemistry, 2012Co-Authors: Kamal H Mroue, Neil Mackinnon, Peizhi Zhu, Erin M B Mcnerny, David H Kohn, Michael D Morris, Ayyalusamy RamamoorthyAbstract:The hierarchical Heterogeneous Architecture of bone imposes significant challenges to structural and dynamic studies conducted by traditional biophysical techniques. High-resolution solid-state nuclear magnetic resonance (SSNMR) spectroscopy is capable of providing detailed atomic-level structural insights into such traditionally challenging materials. However, the relatively long data-collection time necessary to achieve a reliable signal-to-noise ratio (S/N) remains a major limitation for the widespread application of SSNMR on bone and related biomaterials. In this study, we attempt to overcome this limitation by employing the paramagnetic relaxation properties of copper(II) ions to shorten the ¹H intrinsic spin–lattice (T₁) relaxation times measured in natural-abundance ¹³C cross-polarization (CP) magic-angle-spinning (MAS) NMR experiments on bone tissues for the purpose of accelerating the data acquisition time in SSNMR. To this end, high-resolution solid-state ¹³C CPMAS experiments were conducted on type I collagen (bovine tendon), bovine cortical bone, and demineralized bovine cortical bone, each in powdered form, to measure the ¹H T₁ values in the absence and in the presence of 30 mM Cu(II)(NH₄)₂EDTA. Our results show that the ¹H T₁ values were successfully reduced by a factor of 2.2, 2.9, and 3.2 for bovine cortical bone, type I collagen, and demineralized bone, respectively, without reducing the spectral resolution and thus enabling faster data acquisition. In addition, paramagnetic quenching of particular ¹³C NMR resonances on exposure to Cu²⁺ ions in the absence of mineral was also observed, potentially suggesting the relative proximity of three main amino acids in the protein backbone (glycine, proline, and alanine) to the bone mineral surface.
