Assignment of the backbone1H and15N NMR resonances and secondary structure characterization of barstar
- 11 October 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 332 (1-2) , 81-87
- https://doi.org/10.1016/0014-5793(93)80489-h
Abstract
Barstar, a polypeptide inhibitor of ribonucleases, has been studied by 2D and 3D NMR techniques using uniformly 15N-labeled protein. Backbone (15NH-CαH-CβH) resonances were assigned for all but 5 of the 89 residues. Dihedral angle and deuterium exchange studies were used in conjunction with medium range inter-proton NOEs to characterize the secondary structure of barstar. The protein is composed of four α-helices and three short stretches of extended strand. By further analysis of the NOE data three of the helices were found to be parallel to each other with the single disulphide bond linking the second and fourth helices at their C-terminal endsKeywords
This publication has 13 references indexed in Scilit:
- Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineeringBiochemistry, 1993
- Precise vicinal coupling constants3JHNα in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experimentsJournal of Biomolecular NMR, 1992
- Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopyBiochemistry, 1991
- Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three-dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1.beta.Biochemistry, 1989
- Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteinsBiochemical and Biophysical Research Communications, 1983
- Molecular structure of a new family of ribonucleasesNature, 1982
- A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromoleculesBiochemical and Biophysical Research Communications, 1980
- Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopyChemical Physics Letters, 1980
- Investigation of exchange processes by two-dimensional NMR spectroscopyThe Journal of Chemical Physics, 1979
- Two-dimensional spectroscopy. Application to nuclear magnetic resonanceThe Journal of Chemical Physics, 1976