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  2. Nuclear magnetic resonance spectroscopy of proteins

    en.wikipedia.org/wiki/Nuclear_magnetic_resonance...

    One important problem using homonuclear nuclear magnetic resonance is overlap between peaks. This occurs when different protons have the same or very similar chemical shifts. This problem becomes greater as the protein becomes larger, so homonuclear nuclear magnetic resonance is usually restricted to small proteins or peptides. [citation needed]

  3. Nucleic acid structure determination - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_structure...

    Nucleic acid NMR is the use of NMR spectroscopy to obtain information about the structure and dynamics of nucleic acid molecules, such as DNA or RNA. As of 2003, nearly half of all known RNA structures had been determined by NMR spectroscopy. [2] Nucleic acid NMR uses similar techniques as protein NMR, but has several differences.

  4. Nuclear magnetic resonance crystallography - Wikipedia

    en.wikipedia.org/wiki/Nuclear_magnetic_resonance...

    Nuclear magnetic resonance crystallography (NMR crystallography) is a method which utilizes primarily NMR spectroscopy to determine the structure of solid materials on the atomic scale. Thus, solid-state NMR spectroscopy would be used primarily, possibly supplemented by quantum chemistry calculations (e.g. density functional theory ), [ 1 ...

  5. Nuclear magnetic resonance spectroscopy - Wikipedia

    en.wikipedia.org/wiki/Nuclear_magnetic_resonance...

    A 900 MHz NMR instrument with a 21.1 T magnet at HWB-NMR, Birmingham, UK. Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique based on re-orientation of atomic nuclei with non-zero nuclear spins in an external magnetic field.

  6. Nuclear magnetic resonance - Wikipedia

    en.wikipedia.org/wiki/Nuclear_magnetic_resonance

    Bruker 700 MHz nuclear magnetic resonance (NMR) spectrometer. Nuclear Magnetic Resonance (NMR) basic principles. Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are disturbed by a weak oscillating magnetic field (in the near field [1]) and respond by producing an electromagnetic signal with a frequency characteristic of the magnetic ...

  7. Two-dimensional nuclear magnetic resonance spectroscopy

    en.wikipedia.org/wiki/Two-dimensional_nuclear...

    While 1D NMR is more straightforward and ideal for identifying basic structural features, COSY enhances the capabilities of NMR by providing deeper insights into molecular connectivity. The two-dimensional spectrum that results from the COSY experiment shows the frequencies for a single isotope , most commonly hydrogen ( 1 H) along both axes.

  8. Chemical shift index - Wikipedia

    en.wikipedia.org/wiki/Chemical_shift_index

    Example of chemical shift index. The chemical shift index or CSI is a widely employed technique in protein nuclear magnetic resonance spectroscopy that can be used to display and identify the location (i.e. start and end) as well as the type of protein secondary structure (beta strands, helices and random coil regions) found in proteins using only backbone chemical shift data [1] [2] The ...

  9. Intrinsically disordered proteins - Wikipedia

    en.wikipedia.org/wiki/Intrinsically_disordered...

    [4] [51] There are different approaches for predicting IDP structure, such as neural networks or matrix calculations, based on different structural and/or biophysical properties. Many computational methods exploit sequence information to predict whether a protein is disordered. [52] Notable examples of such software include IUPRED and Disopred.