Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides.
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.
Pal-Bhowmick
Ipsita
I
Tata Institute of Fundamental Research, Colaba, Mumbai 400005, India.
Pandey
Ramendra Pati
RP
Jarori
Gotam K
GK
Kar
Santosh
S
Sahal
Dinkar
D
D000595:Amino Acid Sequence; D001665:Binding Sites; D010446:Peptide Fragments / Q000737:chemistry* / Q000276:immunology* / Q000648:ultrastructure; D011485:Protein Binding; D012260:Ribonucleases / Q000737:chemistry* / Q000276:immunology* / Q000648:ultrastructure; D013329:Structure-Activity Relationship; D013601:T-Lymphocytes / Q000276:immunology*
D010446:Peptide Fragments; C023560:ribonuclease S-peptide; D012260:Ribonucleases; C022542:ribonuclease S