A study of the dynamic state of histidine residues in tryptophan synthetase subunit by 13 C nuclear magnetic resonance
| Autor: | D. M. Wilson, H. Sternlicht, G.L. Kenyon, Douglas T. Browne, E. L. Packer |
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| Rok vydání: | 1973 |
| Předmět: |
Magnetic Resonance Spectroscopy
Chemical Phenomena Biophysics Matrix (biology) medicine.disease_cause Biochemistry Nuclear magnetic resonance medicine Escherichia coli Tryptophan Synthase Histidine Molecular Biology Hydro-Lyases chemistry.chemical_classification Α subunit Carbon Isotopes Spectrum Analysis Tryptophan Sodium Dodecyl Sulfate Cell Biology Deuterium Chemistry Enzyme chemistry Electrophoresis Polyacrylamide Gel |
| Zdroj: | Biochemical and biophysical research communications. 50(1) |
| ISSN: | 0006-291X |
| Popis: | Tryptophan synthetase α subunit in which the histidine C 2 (ring) positions are enriched in 13 C and labeled with deuterium was prepared by incorporation of labeled histidine into protein of Escherichia coli . 13 C nuclear magnetic resonance studies of the specifically labeled enzyme demonstrate that all four histidine residues of α subunit are highly immobilized within the protein matrix. |
| Databáze: | OpenAIRE |
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