PubMed Health⌕ Search

PubMed · 16940479

A sensitive method for measuring spatial orientation in bone structures.

Abstract

OBJECTIVES: This article introduces the newly developed line frequency deviation (LFD) method for measuring the orientation of the trabecular structure and shows that it is more sensitive than the mean intercept length (MIL) method that is commonly used. METHODS: The LFD method, which has been developed to measure the orientation of bone on two-dimensional X-ray images, was expanded to handle three-dimensional shapes. For the purpose of comparison, both the LFD and the MIL methods were applied to micro CT scans of 24 trabecular bone samples as well as to 24 simple synthetic samples. LFD and MIL values were calculated in various directions and collected in polar plots. Next, the anisotropy was quantified by calculating the coefficient of variation as well as by fitting ellipsoids through the plots. RESULTS: The MIL method yielded smooth rather spherical ellipsoidal polar plots with almost no sensitivity for changes in structure. The LFD method yielded more slender polar plots and more sensitivity for geometrical changes. The LFD method yielded significantly more anistropy and larger variation in anisotropy. CONCLUSIONS: The LFD method is a more sensitive descriptor of spatial orientation of bone structures than the MIL method.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

W G M Geraets, L J van Ruijven, J G C Verheij, T M G J van Eijden, P F van der Stelt. 2006. A sensitive method for measuring spatial orientation in bone structures.. https://doi.org/10.1259/dmfr%2F50217408

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Protein dynamics from X-ray crystallography: anisotropic, global motion in diffuse scattering patterns.

Understanding X-ray crystallographic diffuse scattering is likely to improve our comprehension of equilibrium collective protein dynamics. Here, using molecular dynamics (MD) simulation, a detailed analysis is performed of the origins of diffuse scattering in crystalline Staphylococcal nuclease, for which the complete diffuse scattering pattern has been determined experimentally. The hydrogen-atom contribution and the scattering range over which the scattering can be considered to be a sum of solvent and protein scattering are determined. Two models of correlated protein motion are investigated by calculating the model-derived diffuse scattering and comparing with the scattering calculated directly from MD trajectories. In one model, previously used in diffuse scattering interpretation, the atomic displacement correlations decay isotropically with increasing separation. Model correlation lengths are obtained by refining the model scattering against the simulation-derived scattering pattern, and are found to be significantly different from those correlation lengths derived directly from the MD trajectories. Furthermore, the convergence between the model-derived and MD-derived scattering is poor. The second model, in which the displacement correlations are calculated from the principal components of the MD trajectories, is capable of fully reproducing the MD-derived diffuse scattering if the approximately 50% lowest-frequency modes are included. However, a small number ( approximately 10) of lowest-frequency and largest-amplitude modes dominates the diffuse scattering and thus the correlated protein motions. A detailed analysis of the principal components is performed. In particular, the effective free energy profile associated with each principle mode is analyzed and the eigenfrequency and damping coefficient computed using a model of Brownian dynamics. Those collective modes with effective frequencies below approximately 0.5 THz, including those that determine the diffuse scattering, are overdamped.

Anisotropy↗

(39)K NMR of solid potassium salts at 21 T: effect of quadrupolar and chemical shift tensors.

39K Solid State NMR spectra (static and magic angle spinning (MAS)) on a set of potassium salts measured at 21.14 T show that the chemical shift range for K(+) ions in diamagnetic salts is well in excess of 100 ppm contrary to previous assumptions that it was quite small. Inequivalent potassium sites in crystals can be resolved through differences in chemical shifts, with chemically similar sites showing differences of over 10 ppm. The quadrupolar coupling constants obtained from MAS and solid echo experiments on powders cover the range from zero for potassium in cubic environments in halides to over 3 MHz for the highly asymmetric sites in K2CO3. Although the quadrupolar effects generally dominate the 39K spectra, in several instances, we have observed subtle but significant contributions of chemical shift anisotropy with values up to 45 ppm, a first such observation. Careful analysis of static and MAS spectra allows the observation of the various chemical shift and quadrupole coupling tensor components as well as their relative orientations, thereby demonstrating that high-field 39K NMR spectroscopy in the solid state has a substantial sensitivity to the local environment with parameters that will be of considerable value in materials characterization and electronic structure studies.

Anisotropy↗