PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 15953742

Structural anisotropy and internal magnetic fields in trabecular bone: coupling solution and solid dipolar interactions.

Louis-S Bouchard·Felix W Wehrli·Chih-Liang Chin·Warren S Warren
View original source ↗Export metadata ↓

Abstract

We investigate the use of intermolecular multiple-quantum coherence to probe structural anisotropy in trabecular bone. Despite the low volume fraction of bone, the bone-water interface produces internal magnetic field gradients which modulate the dipolar field, depending on sample orientation, choice of dipolar correlation length, correlation gradient direction, and evolution time. For this system, the probing of internal magnetic field gradients in the liquid phase permits indirect measurements of the solid phase dipolar field. Our results suggest that measurements of volume-averaged signal intensity as a function of gradient strength and three orthogonal directions could be used to non-invasively measure the orientation of structures inside a sample or their degree of anisotropy. The system is modeled as having two phases, solid and liquid (bone and water), which differ in their magnetization density and magnetic susceptibility. A simple calculation using a priori knowledge of the material geometry and distribution of internal magnetic fields verifies the experimental measurements as a function of gradient strength, direction, and sample orientation.

Explore related subjects

AnisotropyHumansMagnetic Resonance SpectroscopyPhantoms, ImagingPorosityTibiaJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Louis-S Bouchard, Felix W Wehrli, Chih-Liang Chin, Warren S Warren. 2005. Structural anisotropy and internal magnetic fields in trabecular bone: coupling solution and solid dipolar interactions.. https://doi.org/10.1016/j.jmr.2005.05.012

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

KEEP EXPLORING

Related citations

PubMed2006

Resolution enhancement in spectra of natural products dissolved in weakly orienting media with the help of 1H homonuclear dipolar decoupling during acquisition: application to 1H-13C dipolar couplings measurements.

In weakly orienting media such as poly-gamma-benzyl-L-glutamate (PBLG) a polymer that forms a chiral liquid crystal in organic solvents, the spectral resolution for embedded molecules is usually poor because of numerous (1)H, (1)H dipolar couplings that generally broaden proton spectra. Therefore (1)H, (13)C dipolar couplings are difficult or impossible to measure. Here, we incorporate Flip-Flop decoupling during detection into an HSQC experiment. Flip-Flop removes the (1)H, (1)H dipolar couplings and scales the chemical shifts of the protons as well as the (1)H, (13)C dipolar couplings during detection. A resolution gain by a factor 1.5-4.2 and improved signal intensity by an average factor of 1.6-1.7 have been obtained. This technique is demonstrated on (+)-menthol dissolved in a PBLG/CDCl(3) phase.

Anisotropy↗
PubMed2006

On the mechanism of nucleosome assembly by histone chaperone NAP1.

The process of mononucleosome assembly mediated by histone chaperone NAP1 was investigated using DNA fragments 146 and 207 bp in length containing the Lytechinus variegatus 5 S rDNA nucleosome positioning sequence. A quantitative description was derived using gel electrophoresis and fluorescent anisotropy data. First, NAP1-bound H3.H4 was released forming a DNA-histone tetramer complex with a time constant of k(1) = (2.5 +/- 0.7) . 10(4) m(-1) s(-1). The tetrasome was converted quickly (k(2) = (4.1 +/- 3.5) . 10(5) m(-1) s(-1)), by the addition of a single H2A.H2B dimer, into a "hexasome," i.e. a nucleosome lacking one H2A.H2B dimer. From this intermediate a nucleosome was formed by the addition of a second H2A.H2B dimer with an average rate constant k(3) = (6.6 +/- 1.4) . 10(3) m(-1) s(-1). For the back-reaction, significant differences were observed between the 146- and 207-bp DNA upon substitution of the canonical H2A histone with H2A.Z. The distinct nucleosome/hexasome ratios were reflected in the corresponding equilibrium dissociation constants and revealed some differences in nucleosome stability. In a fourth reaction, NAP1 mediated the binding of linker histone H1 to the nucleosome, completing the chromatosome structure with k(4) = (7.7 +/- 3.7) . 10(3) m(-1) s(-1). The activity of the chromatin remodeling complex ACF did not increase the kinetics of the mononucleosome assembly process.

Anisotropy↗
PubMed2006

Mechanism of a hereditary cataract phenotype. Mutations in alphaA-crystallin activate substrate binding.

We present a novel hypothesis for the molecular mechanism of autosomal dominant cataract linked to two mutations in the alphaA-crystallin gene of the ocular lens. AlphaA-crystallin is a molecular chaperone that plays a critical role in the suppression of protein aggregation and hence in the long term maintenance of lens optical properties. Using a steady state binding assay in which the chaperone-substrate complex is directly detected, we demonstrate that the mutations result in a substantial increase in the level of binding to non-native states of the model substrate T4 lysozyme. The structural basis of the enhanced binding is investigated through equivalent substitutions in the homologous heat shock protein 27. The mutations shift the oligomeric equilibrium toward a dissociated multimeric form previously shown to be the binding-competent state. In the context of a recent thermodynamic model of chaperone function that proposes the coupling of small heat shock protein activation to the substrate folding equilibrium (Shashidharamurthy, R., Koteiche, H. A., Dong, J., and McHaourab, H. S. (2005) J. Biol. Chem. 280, 5281-5289), the enhanced binding by the alphaA-crystallin mutants is predicted to shift the substrate folding equilibrium toward non-native intermediates, i.e. the mutants promote substrate unfolding. Given the high concentration of alphaA-crystallin in the lens, the molecular basis of pathogenesis implied by our results is a gain of function that leads to the binding of undamaged proteins and subsequent precipitation of the saturated alpha-crystallin complexes in the developing lens of affected individuals.

Anisotropy↗