Isolation and complete amino acid sequence of the β- and α-polypeptides from the peripheral light-harvesting pigment-protein complex II ofRhodobacter sulfidophilus
| Autor: | Monier H. Tadros, Gesine E. Hagemann, Roland Dierstein, Emile Schiltz, Eleni Katsiou |
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| Rok vydání: | 1995 |
| Předmět: |
Photosynthetic reaction centre
Molecular Sequence Data Photosynthetic Reaction Center Complex Proteins Light-Harvesting Protein Complexes Biophysics Biochemistry LHII Light-harvesting complex chemistry.chemical_compound Bacterial Proteins α-Polypeptide Structural Biology β-Polypeptide Genetics Trifluoroacetic acid Amino Acid Sequence Rhodobacter Sodium dodecyl sulfate Molecular Biology Peptide sequence Polyacrylamide gel electrophoresis Chromatography High Pressure Liquid Molecular mass biology Chemistry Cell Membrane Cell Biology biology.organism_classification Peptide Fragments Molecular Weight Rhodobacter sulfidophilus Sequence Analysis |
| Zdroj: | FEBS Letters. 368:243-247 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(95)00645-p |
| Popis: | The peripheral light-harvesting bacteriochlorophyll-carotenoid-protein complex B800-850 (LHII) has been isolated from membranes of semi-aerobic dark-grown cells of Rhodobacter sulfidophilus strain W4. A reversed-phase HPLC system resolved one beta- and one alpha-polypeptide in the ratio 1:1. The material obtained was of high purity and suitable for direct microsequence analysis. The primary structures of the beta- and alpha-polypeptides have been determined. The beta-polypeptide consists of 51 amino acid residues, yielding a molecular mass of 5512 Da and having 64.7% hydrophobicity. The alpha-polypeptide consists of 52 amino acid residues, with a calculated molecular mass of 5661 Da and 75% hydrophobicity. The significance of uncommon structure motives with respect to the unusual spectroscopic characteristics of this light-harvesting complex is discussed. |
| Databáze: | OpenAIRE |
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