Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides
Autor: | Ramendra Pati Pandey, Santosh K. Kar, Ipsita Pal-Bhowmick, Dinkar Sahal, Gotam K. Jarori |
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Rok vydání: | 2007 |
Předmět: |
endocrine system
Stereochemistry T cell T-Lymphocytes Biophysics Peptide Biochemistry Structure-Activity Relationship Molecular recognition Ribonucleases medicine Functional studies Ribonuclease RNase activity Retro inverso Amino Acid Sequence Molecular Biology chemistry.chemical_classification Binding Sites biology Cell Biology Peptide Fragments Complementation medicine.anatomical_structure chemistry biology.protein Protein Binding |
Zdroj: | Biochemical and biophysical research communications. 364(3) |
ISSN: | 1090-2104 |
Popis: | Ribonuclease S peptide and S protein offer a unique complementation system to understand the finer features of molecular recognition. In the present study the S peptide (1-16), and its retro and retro-inverso analogs have been analyzed for their structural and biological attributes. RPHPLC, CD, and NMR analyses have revealed that the physicochemical and conformational properties of the S peptide are distinct from those of its retro and retro-inverso analogs. On the functional side, while the S peptide complemented the S protein to give RNase activity, was recognized by anti-S peptide antibodies and induced T cell proliferation, neither the retro nor the retro-inverso S peptides could do so. |
Databáze: | OpenAIRE |
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