NMR- Based Structure Determination of Proteins in Solution

  • Andrzej Ejchart
  • Igor Zhukov
Part of the Springer Protocols Handbooks book series (SPH)


Nuclear magnetic resonance (NMR) spectroscopy is well suited to play an important part in proteomics programs because this method provides structural information at the atomic level. Nuclei of isotopes of biologically important elements display narrow reso- nance lines. Internuclear interactions, modulated by even small structural and confor- mational changes, influence line position, line shape, and intensity of signals in NMR spectra. Last but not least, NMR provides high-resolution structures in solution, allow- ing the study of proteins that fail to crystallize or comparison of differences between their crystal and solution structure (1). The potential of the NMR method, however, has not been reflected by the present number of deposited structures; less than 14% of the protein structures in the Protein Data Bank (PDB) have been determined by NMR spec- troscopy (2).


Nuclear Magnetic Resonance Dihedral Angle Nuclear Magnetic Resonance Spectrum Nuclear Magnetic Resonance Spectroscopy Scalar Coupling 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Humana Press Inc., Totowa, NJ 2005

Authors and Affiliations

  • Andrzej Ejchart
    • 1
  • Igor Zhukov
    • 2
  1. 1.Institute of Biochemistry and BiophysicsPoland
  2. 2.Institute of Biochemistry and BiophysicsWarsawPoland

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