NMR Studies of Structure and Conformation in Peptides and Proteins

  • K. Wüthrich
Part of the NATO Advanced Study Institutes Series book series (NSSB, volume 22)


Investigations of the relations between covalent structure, molecular conformations and functional properties of biological macromolecules play a prominent role in modern biochemistry, molecular biology, and biophysics. While chemical methods have so far served to unravel the covalent structures of a large number of biopolymers [1], and X-ray crystallography in single crystals has set the standards for the description of the three-dimensional conformations in these molecules [2], NMR has become an attractive technique for investigations of the molecular conformations in solution. To a large extent the high sensitivity and high resolution required for biological applications of NMR have become available by recent advances in apparatus design and biochemical methods, i.e. on the one hand the introduction of superconducting magnets and Fourier transform techniques into the modern NMR spectrometers, on the other hand the preparation of isotope-labelled biopolymers, by chemical and biosynthetic techniques. In the present lecture, some basic notions on structure and conformation of one class of biopolymers, i.e. peptides and proteins, will be introduced, and the manifestations in the NMR parameters of different molecular structures and conformations will be discussed and illustrated with some selected examples.


Torsion Angle Polypeptide Chain Random Coil Amino Acid Side Chain Molecular Conformation 


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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • K. Wüthrich
    • 1
  1. 1.Eidgenössische Technische HochschuleZürichSwitzerland

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