A hydrophobic tryptic peptide from bovine white matter proteolipid
| Autor: | James J. L'italien, Marjorie B. Lees, Richard A. Laursen, Betty H. Chao |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Proteolipid protein 1
Proteolipids Biophysics Peptide Biochemistry Mass Spectrometry chemistry.chemical_compound Structural Biology Animals Trypsin Amino Acid Sequence Cyanogen Bromide Molecular Biology Protein secondary structure Peptide sequence Brain Chemistry chemistry.chemical_classification Edman degradation Protein primary structure Proteolytic enzymes Peptide Fragments Molecular Weight chemistry Cattle Cyanogen bromide |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 702:117-124 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(82)90034-6 |
| Popis: | A hydrophobic, chloroform-soluble tryptic peptide with a molecular weight of approximately 4000 has been purified from the bovine white matter proteolipid protein. Its primary structure was obtained by a combination of solid-phase Edman degradation and mass spectrometry. A major part of the tryptic peptide appears to be inaccessible to the action of proteolytic enzymes. The peptide spans the three cyanogen bromide peptides located by Jollès et al. (Biochem. Biophys. Res. Commun. (1979) 87, 619--626) at the COOH-terminal region of the intact protein. Secondary structure calculations for this region indicate a segregation into discrete domains, with most of the tryptic peptide corresponding to a highly ordered, hydrophobic domain; an equal probability for alpha-helical or beta-structure is predicted for this region. |
| Databáze: | OpenAIRE |
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