Toward automated determination of buildup rates of nuclear overhauser effects in proteins, using symmetry projection operators
- 1 October 1990
- journal article
- research article
- Published by Elsevier in Journal of Magnetic Resonance (1969)
- Vol. 89 (3) , 585-594
- https://doi.org/10.1016/0022-2364(90)90343-8
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Trapping folding intermediatesNature, 1988
- Secondary structure of barley serine proteinase inhibitor 2 determined by proton nuclear magnetic resonance spectroscopyCarlsberg Research Communications, 1987
- Sequence specific assignment of the proton nuclear magnetic resonance spectrum of barley serine proteinase inhibitor 2Carlsberg Research Communications, 1987
- Symmetry recognition applied to two-dimensional NMR dataCarlsberg Research Communications, 1987
- Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seedsBiochemistry, 1987
- Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2Protein Engineering, Design and Selection, 1987
- Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopyProtein Engineering, Design and Selection, 1987
- The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamicsProtein Engineering, Design and Selection, 1987
- 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
- Characteristics of hiproly barley I. Isolation and characterisation of two water-soluble high-lysine proteinsCarlsberg Research Communications, 1980