ABSTRACT
The interaction of the oligopeptides Ala-Gln-GIn-Leu-Ala-Gly-OH and Gln-Leu- Ala-Gly-OMe corresponding, respectively, to the sequence 53–58 and 55–58 of lac repressor protein with four polynucleotides was studied. The two peptides did not interact with poly dA. poly dT, poly d(A-T).poly d(A-T) or poly d(A-G).poly d(C-T). But they interacted in a characteristic way with poly d(A-C). poly d (G-T), the sequences of which are in abundance in the lac operator region. Both the peptides stabilised the melting of poly d (A-C). poly d (G-T) at a peptide to nucleotide ratio (P/N) of 4; at lower ratios, they destabilised the DNA slightly. The circular dichroism of the alternating polynucleotide with CAC/GTG sequences was perturbed by both the oligopeptides. The hexapeptide at a P/N of 4 caused the transformation of the Bform circular dichroism spectrum to a new state, characterised by strong 220 and 240 nm bands, and a rather weak long wavelength spectrum.
ABSTRACT
Using the lectin-concanavalin-A, the tryptophan fluorescence as a function of pH was studied. The pH dependent, fluorescence intensity changes were significantly higher when excited at 305 nm, than when irradiated at 280nm. Only one tryptophanyl per monomer of concanavalin-A was available for oxidation by N-bromosuccinimide in the dimeric form at pH 4·9; no tryptophanyl could be oxidised in the demetallised dimer (pH 3·0) and native tetramer (pH 7·0). Based on this fluorescence data and the already known crystal structure data, it appears that tryptophanyl 88 in concanavalin-A may be selectively excited by 305 nm radiation.