The structure of crystalline Escherichia coli-derived rat intestinal fatty acid-binding protein at 2.5-A resolution.
Open Access
- 1 April 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (12) , 5815-5819
- https://doi.org/10.1016/s0021-9258(18)60638-6
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- “Homology” in proteins and nucleic acids: A terminology muddle and a way out of itCell, 1987
- The Metabolic Significance of Mammalian Fatty-Acid-Binding Proteins: Abundant Proteins in Search of a FunctionAnnual Review of Nutrition, 1987
- One fold among manyNature, 1987
- The structure of β-lactoglobulin and its similarity to plasma retinol-binding proteinNature, 1986
- Analyzing the structures, functions and evolution of two abundant gastrointestinal fatty acid binding proteins with recombinant DNA and computational techniquesChemistry and Physics of Lipids, 1985
- [19] Oscillation method with large unit cellsPublished by Elsevier ,1985
- The ROCKS system of computer programs for macromolecular crystallographyJournal of Applied Crystallography, 1984
- Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functionsActa Crystallographica Section A Foundations of Crystallography, 1983
- [47] Establishing homologies in protein sequencesPublished by Elsevier ,1983
- Similar Amino Acid Sequences: Chance or Common Ancestry?Science, 1981