Nuclear magnetic resonance solution and X-ray structures of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop
- 1 December 1989
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 210 (3), 649-654
- https://doi.org/10.1016/0022-2836(89)90138-1
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealingJournal of Molecular Biology, 1989
- The refined 2.0 Å X‐ray crystal structure of the complex formed between bovine β‐trypsin and CMTI‐I, a trypsin inhibitor from squash seeds (Cucurbita maxima) Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoesFEBS Letters, 1989
- Improved strategies for the determination of protein structures from NMR data: The solution structure of acyl carrier proteinFEBS Letters, 1989
- Crystallographic refinement by simulated annealingJournal of Molecular Biology, 1988
- 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
- Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determinationJournal of Molecular Biology, 1986
- The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)European Journal of Biochemistry, 1985
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolutionActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1975