NMR of Macromolecules


Nuclear magnetic resonance (NMR) spectroscopy is an analytical tool used to determine the structure and dynamics of molecules. NMR spectroscopy of macromolecules provides information about the three-dimensional structure of proteins and nucleic acids, as well as the dynamics of their interactions with other molecules.

NMR spectroscopy is based on the principle that the nuclei of certain atoms, when placed in a magnetic field, will absorb and emit electromagnetic radiation at specific frequencies. The frequency of the radiation absorbed or emitted by a nucleus is proportional to the strength of the magnetic field and the strength of the nuclear magnetic moment.

The most common nuclei used in NMR spectroscopy are 1H and 13C. The 1H nucleus has a spin of 1/2 and a magnetic moment of 2.79 Bohr magnetons. The 13C nucleus has a spin of 1/2 and a magnetic moment of 0.70 Bohr magnetons.

The strength of the magnetic field is typically in the range of 20 to 40 Tesla. The frequency of the radiation absorbed or emitted by the nucleus is in the radiofrequency range, from about 10 MHz to about 10 GHz.

NMR spectroscopy can be used to determine the structure of a molecule by measuring the distances between the nuclei of the atoms in the molecule. The distances between the atoms can be determined from the frequency of the radiation absorbed or emitted by the nuclei.

NMR spectroscopy can also be used to study the dynamics of molecules. The rate at which a molecule changes its conformation can be determined from the width of the absorption line in the NMR spectrum.

NMR spectroscopy is a powerful tool for the study of macromolecules. By measuring the distances between the nuclei of the atoms in a molecule, NMR spectroscopy can provide information about the three-dimensional structure of the molecule. NMR spectroscopy can also be used to study the dynamics of molecules, providing information about the rate at which the molecule changes its conformation.


Leave a Reply

Your email address will not be published. Required fields are marked *