G01R33/465

IMAGING SYSTEM FOR SINGLE VOXEL SPECTROSCOPY
20170299677 · 2017-10-19 ·

A guide map is created for use in placing a spectroscopic single voxel in a region of interest in single voxel magnetic resonance spectroscopy. An anatomical planning image of the region of interest is obtained through MRI. A spectroscopy voxel is stepped across the region of interest, characteristics of the magnetic field used in the MRI are measured at each location of the imaging voxel, and a guide-FWHM map indicative of the homogeneity/inhomogeneity of the magnetic field over the region of interest is derived using the measurements. The guide map is created by overlaying the guide-FWHM map on the anatomical planning image. A spectroscopic single voxel of a size corresponding to that of the spectroscopy voxel is placed within the region of interest as per the guide map. Then spectral data is acquired from the region of interest confined to the single voxel.

Multi-parameter diabetes risk evaluations

Methods, systems and circuits evaluate a subject's risk of developing type 2 diabetes or having prediabetes using at least one defined mathematical model of risk of progression that can stratify risk for patients having the same glucose measurement. The model may include NMR derived measurements of GlycA and a plurality of selected lipoprotein components of at least one biosample of the subject.

Multi-parameter diabetes risk evaluations

Methods, systems and circuits evaluate a subject's risk of developing type 2 diabetes or having prediabetes using at least one defined mathematical model of risk of progression that can stratify risk for patients having the same glucose measurement. The model may include NMR derived measurements of GlycA and a plurality of selected lipoprotein components of at least one biosample of the subject.

TENSOR FIELD MAPPING

During operation, a system may apply an external magnetic field and an RF pulse sequence to a sample. Then, the system may measure at least a component of a magnetization associated with the sample, such as MR signals of one or more types of nuclei in the sample. Moreover, the system may calculate at least a predicted component of the magnetization for voxels associated with the sample based on the measured component of the magnetization, a forward model, the external magnetic field and the RF pulse sequence. Next, the system may solve an inverse problem by iteratively modifying the parameters associated with the voxels in the forward model until a difference between the predicted component of the magnetization and the measured component of the magnetization is less than a predefined value. Note that the calculations may be performed concurrently with the measurements and may not involve performing a Fourier transform.

RAPID DETERMINATION OF A RELAXATION TIME

During operation, a system may apply a polarizing field and an excitation sequence to a sample. Then, the system may measure a signal associated with the sample for a time duration that is less than a magnitude of a relaxation time associated with the sample. Next, the system may calculate the relaxation time based on a difference between the measured signal and a predicted signal of the sample, where the predicted signal is based on a forward model, the polarizing field and the excitation sequence. After modifying at least one of the polarizing field and the excitation sequence, the aforementioned operations may be repeated until a magnitude of the difference is less than a convergence criterion. Note that the calculations may be performed concurrently with the measurements and may not involve performing a Fourier transform on the measured signal.

Enhanced nuclear spin polarization

The polarization of nuclear spins of a material may be enhanced by encapsulating the material within a reverse micelle.

Enhanced nuclear spin polarization

The polarization of nuclear spins of a material may be enhanced by encapsulating the material within a reverse micelle.

METHOD AND SYSTEM FOR DETECTING AND CONTROLLING LONG-RANGE QUANTUM COHERENCE OF MOLECULAR INTERACTIONS
20220042937 · 2022-02-10 · ·

The present disclosure provides a method and system for detecting and controlling the long-range quantum coherence of molecular interactions, e.g., hydrogen bonds, with an electrical current or electromagnetic field, e.g., in a low end of radio frequency range at room temperature. The resonant frequencies of molecular interactions such as hydrogen bonds may be detected and the long-range quantum coherence of the molecular interactions such as hydrogen bonds may be controlled with electrical current or electromagnetic fields.

Stable isotope-labeled aliphatic amino acid and NMR structural analysis of protein using same

Provided is a stable isotope-labeled aliphatic amino acid enabling the assignment of the signal of an amino acid residue side chain by increasing to the maximum the observation sensitivity to an NMR signal of the same amino acid residue side chain, and allowing NOE (nuclear Overhauser effect) between protons in the amino acid residue to be observed. The stable isotope-labeled aliphatic amino acid is for constituting a protein and satisfies all of the following conditions (1) to (3): (1) two or more carbon atoms are labeled with .sup.13C; (2) of two or more carbon atoms labeled with .sup.13C, a carbon atom other than a carbon atom of a methyl group, which is capable of bonding to a hydrogen atom, has one .sup.1H directly bonded thereto, while the carbon atom of the methyl group has at least one .sup.1H directly bonded thereto; and (3) other carbon atoms adjacent to all the .sup.13C are all .sup.12C.

Stable isotope-labeled aliphatic amino acid and NMR structural analysis of protein using same

Provided is a stable isotope-labeled aliphatic amino acid enabling the assignment of the signal of an amino acid residue side chain by increasing to the maximum the observation sensitivity to an NMR signal of the same amino acid residue side chain, and allowing NOE (nuclear Overhauser effect) between protons in the amino acid residue to be observed. The stable isotope-labeled aliphatic amino acid is for constituting a protein and satisfies all of the following conditions (1) to (3): (1) two or more carbon atoms are labeled with .sup.13C; (2) of two or more carbon atoms labeled with .sup.13C, a carbon atom other than a carbon atom of a methyl group, which is capable of bonding to a hydrogen atom, has one .sup.1H directly bonded thereto, while the carbon atom of the methyl group has at least one .sup.1H directly bonded thereto; and (3) other carbon atoms adjacent to all the .sup.13C are all .sup.12C.