Systematic Application of Two‐Dimensional 1H Nuclear‐Magnetic‐Resonance Techniques for Studies of Proteins
- 1 February 1981
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 114 (2), 365-374
- https://doi.org/10.1111/j.1432-1033.1981.tb05156.x
Abstract
This and the following paper describe the practical application of recently developed, two-dimensional nuclear magnetic resonance techniques for studies of proteins. In the present report spin-echo-correlated spectroscopy and two-dimensional J-resolved spectroscopy are used to identify complete spin systems of non-labile, aliphatic protons in the basic pancreatic trypsin inhibitor. Overall, 41 out of the 58 aliphatic spin systems in this protein were identified; for the first time the spin systems of all the glycyl residues in a protein have been identified in the 1H NMR spectrum. Combined with the following paper, the present data yield new individual assignments for numerous amino acid residues and provide a new avenue, based on accurate measurements of spin-spin coupling constants in the two-dimensional J-resolved spectra, for studying changes of static and dynamic aspects of protein conformation between single crystals and solution, or between different conditions of solvent and temperature.Keywords
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