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Mass spectrometry is a scientific technique for measuring the mass-to-charge ratio of ions. It is often coupled to chromatographic techniques such as gas-or liquid chromatography and has found widespread adoption in the fields of analytical chemistry and biochemistry where it can be used to identify and characterize small molecules and proteins ().
In solid-state NMR spectroscopy, magic-angle spinning (MAS) is a technique routinely used to produce better resolution NMR spectra. MAS NMR consists in spinning the sample (usually at a frequency of 1 to 130 kHz) at the magic angle θ m (ca. 54.74°, where cos 2 θ m =1/3) with respect to the direction of the magnetic field.
Such limitation of non-targeted analysis makes it less suitable for analyzing highly complex, highly dynamic sample such as human blood serum. [2] However, the methods of utilizing targeted mass spectrometry are still at a primitive stage, in the sense that the inclusion list used in the targeted analysis is typically manually typed-in by ...
Marker assisted selection or marker aided selection (MAS) is an indirect selection process where a trait of interest is selected based on a marker (morphological, biochemical or DNA/RNA variation) linked to a trait of interest (e.g. productivity, disease resistance, abiotic stress tolerance, and quality), rather than on the trait itself.
The analysis of 'stable isotopes' is normally concerned with measuring isotopic variations arising from mass-dependent isotopic fractionation in natural systems. On the other hand, radiogenic isotope analysis [3] involves measuring the abundances of decay-products of natural radioactivity, and is used in most long-lived radiometric dating methods.
The velocity of the charged particle after acceleration will not change since it moves in a field-free time-of-flight tube. The velocity of the particle can be determined in a time-of-flight tube since the length of the path (d) of the flight of the ion is known and the time of the flight of the ion (t) can be measured using a transient digitizer or time to digital converter.
The chart portion of the forest plot will be on the right hand side and will indicate the mean difference in effect between the test and control groups in the studies. A more precise rendering of the data shows up in number form in the text of each line, while a somewhat less precise graphic representation shows up in chart form on the right.
Top-down vs bottom-up proteomics. Top-down proteomics is a method of protein identification that either uses an ion trapping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry (MS/MS) analysis [1] [2] or other protein purification methods such as two-dimensional gel electrophoresis in conjunction with MS/MS. [3] Top-down proteomics is capable ...