Circular dichroism studies on the proline-rich glycoprotein of human parotid saliva
Autor: | Nicole Porchet, Arnold Boersma, M.H. Loucheux-Lefebvre, Jean-Pierre Aubert, Pierre Degand |
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Rok vydání: | 1982 |
Předmět: |
Glycan
Circular dichroism Proline Protein Conformation Stereochemistry Biophysics Sequence (biology) Biochemistry Structural Biology Humans Parotid Gland Salivary Proteins and Peptides Molecular Biology Protein secondary structure Peptide sequence Glycoproteins Polyproline helix chemistry.chemical_classification biology Circular Dichroism Protein primary structure Peptide Fragments chemistry biology.protein Calcium Glycoprotein |
Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 704:361-365 |
ISSN: | 0167-4838 |
DOI: | 10.1016/0167-4838(82)90166-2 |
Popis: | Previous results on the primary structure of the human parotid saliva proline-rich glycoprotein established the concept of repetitive domains in the sequence of that glycoproteln, tryptic glycopeptides of proline-rich glycoprotein representing the basic structure. The present work is concerned with the study of the secondary structure of the proline-rich glycoprotein, and of tryptic giycopeptides with and without the glycan moiety, using circular dichroism. CD spectra exhibit the same secondary structure with about 60% of polyproline II helical structure for the proline-rich glycoprotein, tryptic glycopeptides and their deglycosylated homologues. The present results are in fair agreement with the amino acid sequence results and suggest a model for the schematic representation of the proline-rich glycoprotein. |
Databáze: | OpenAIRE |
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