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Due to the relatively large differences in IR absorption frequencies that are due to different resonance frequencies for molecules containing different isotopes, this technique has been suggested as a way to perform Isotope separation with difficult-to-separate isotopes, in a single pass.
Nucleic acid NMR is the use of nuclear magnetic resonance spectroscopy to obtain information about the structure and dynamics of nucleic acid molecules, such as DNA or RNA.It is useful for molecules of up to 100 nucleotides, and as of 2003, nearly half of all known RNA structures had been determined by NMR spectroscopy.
Energy-level diagram showing the states involved in Raman spectra. Raman spectroscopy (/ ˈ r ɑː m ən /) (named after physicist C. V. Raman) is a spectroscopic technique typically used to determine vibrational modes of molecules, although rotational and other low-frequency modes of systems may also be observed. [1]
Carbohydrate NMR spectroscopy is the application of nuclear magnetic resonance (NMR) spectroscopy to structural and conformational analysis of carbohydrates.This method allows the scientists to elucidate structure of monosaccharides, oligosaccharides, polysaccharides, glycoconjugates and other carbohydrate derivatives from synthetic and natural sources.
Like ordinary Raman spectroscopy, resonance Raman is compatible with samples in water, which has a very weak scattering intensity and little contribution to spectra. However, the need for an excitation laser with a wavelength matching that of an electronic transition in the analyte of interest somewhat limits the applicability of the method. [8]
Nucleotide analog interference mapping (NAIM) is the process of using nucleotide analogs, molecules that are similar in some ways to nucleotides but lack function, to determine the importance of a functional group at each location of an RNA molecule. [39] [40] The process of NAIM is to insert a single nucleotide analog into a unique site.
The SNIF-NMR method (Site-Specific Natural Isotope Fractionation studied by Nuclear Magnetic Resonance) is able to determine, to a high level of accuracy, the isotopic ratios for each of the sites of the molecule, which enables a better discrimination.
1 H– 15 N HSQC polarization scheme for a protein/amino acid. 1 H– 15 N HSQC spectrum of a fragment of an isotopically labeled protein NleG3-2. Each peak in the spectrum represents a bonded N-H pair, with its two coordinates corresponding to the chemical shifts of each of the H and N atoms.