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Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 1. Combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labile protons in amino-acid residues.
- Source :
-
European journal of biochemistry [Eur J Biochem] 1981 Feb; Vol. 114 (2), pp. 365-74. - Publication Year :
- 1981
-
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.
Details
- Language :
- English
- ISSN :
- 0014-2956
- Volume :
- 114
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- European journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 6163630
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1981.tb05156.x