DOMAIN CLOSURE IN MITOCHONDRIAL ASPARTATE-AMINOTRANSFERASE
- 4 September 1992
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 227 (1), 197-213
- https://doi.org/10.1016/0022-2836(92)90691-C
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- Analysis of protein loop closure: Two types of hinges produce one motion in lactate dehydrogenaseJournal of Molecular Biology, 1991
- Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilusJournal of Molecular Biology, 1988
- Correlation of polarized absorption spectroscopic and X-ray diffraction studies of crystalline cytosolic aspartate aminotransferase of pig heartsJournal of Molecular Biology, 1988
- The primary structure of mitochondrial aspartate aminotransferase from human heartBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structureJournal of Molecular Biology, 1984
- The three-dimensional structure of mitochondrial aspartate aminotransferase at 4.5 Å resolutionJournal of Molecular Biology, 1979
- Conformation of amino acid side-chains in proteinsJournal of Molecular Biology, 1978
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Structural invariants in protein foldingNature, 1975
- The interpretation of protein structures: Total volume, group volume distributions and packing densityJournal of Molecular Biology, 1974