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A 500 MHz proton NMR study of interaction of tripeptides Lys-Tyr-Lys and Lys-Phe-Lys with deoxydinucleotide d-CpG.
Indian J Biochem Biophys ; 1992 Oct; 29(5): 394-401
Article Dans Anglais | IMSEAR | ID: sea-28096
ABSTRACT
The binding of di- and tetranucleotides with tri- and tetrapeptides containing Tyr, Trp, Phe having lysine on both ends has been studied using a 500 MHz proton NMR. The results show that d-CpG exists as a right-handed B-DNA structure with both sugars in 01'-endo sugar conformation and glycosidic bond angle as in anti domain. On binding to tripeptide Lys-Tyr-Lys, the Tyr ring protons shift upfield by 0.015 ppm at 285 degrees K, while the conformation of d-CpG remains unchanged. Change in chemical shift of Tyr and nucleotide protons decreases with temperature. This upfield shift is attributed to stacking with bases/base-pairs. The presence of intermolecular NOE's also supports this. Results of binding of d-CpG to Lys-Phe-Lys are similar to those with Lys-Tyr-Lys except that the chemical shift changes occur to a lesser extent. On comparing the results obtained with three different peptides, it is found that interaction decreases in the order Trp > Tyr > Phe which is similar to that found by theoretical energy calculations (reported elsewhere) and fluorescence measurements. The results also exhibit a specificity in recognition of these amino acid residues by dinucleotides.
Sujets)
Texte intégral: Disponible Indice: IMSEAR (Asie du Sud-Est) Sujet Principal: Oligopeptides / Conformation des protéines / Thermodynamique / Spectroscopie par résonance magnétique / Nucléotides désoxycytidyliques / Désoxyguanosine / Conformation d'acide nucléique langue: Anglais Texte intégral: Indian J Biochem Biophys Année: 1992 Type: Article

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Texte intégral: Disponible Indice: IMSEAR (Asie du Sud-Est) Sujet Principal: Oligopeptides / Conformation des protéines / Thermodynamique / Spectroscopie par résonance magnétique / Nucléotides désoxycytidyliques / Désoxyguanosine / Conformation d'acide nucléique langue: Anglais Texte intégral: Indian J Biochem Biophys Année: 1992 Type: Article