Systematic Application of Two‐Dimensional 1H Nuclear‐Magnetic‐Resonance Techniques for Studies of Proteins

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Abstract
The practical application of recently developed, 2-dimensional NMR techniques for studies of proteins is described. Spin-echo-correlated spectroscopy and 2-dimensional J-resolved spectroscopy are used to identify complete spin systems of non-labile, aliphatic protons in the basic pancreatic trypsin inhibitor. Of the 58 aliphatic spin systems in this protein, 41 were identified; for the 1st time the spin systems of all the glycyl residues in a protein were identified in the 1H NMR spectrum. The 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 2-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.