Nevertheless, the results appear to indicate that the conformation of the bound peptide to the G4s for 5 of the 6 complexes are of the more unordered conformation observed for the Rhau25 peptide in Tris-HCl buffer, while the peptide bound to Htelo1 G-quadruplex sequence appears to bind with a more α-helical conformation, though the base contributions are quite significant.
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Interaction of a Short Peptide with G-Quadruplex-Forming Sequences: An SRCD and CD Study.
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