4-Nitrophenyl phosphoric acid and its four different potassium salts: a solid state structure and kinetic study
The structures of 4-nitrophenyl phosphoric acid, H2NPP (1), and its four different potassium salts, K(H2NPP)(HNPP) (2), K(HNPP)·CH3OH (3), K(HNPP)·2H2O (4), and K2(NPP)·4H2O (5), were determined by X-ray diffraction methods. These investigations, together with the study of the role of potassium ions in the hydrolysis of 4-nitrophenyl phosphate, provided information about interactions between the acid, monoanionic and dianionic forms of 4-nitrophenyl phosphate and the potassium cations. In the crystalline state, the H2NPP molecules form one-dimensional chains of bifurcated O–H⋯O hydrogen bonds between phosphate groups. A different network, derived from ladder-like chains of the O–H⋯O hydroge…
Combined effect of the DeltaPhe or DeltaAla residue and the p-nitroanilide group on a didehydropeptides conformation.
Two series of dehydropeptides of the general formulae Boc-Gly-X-Phe-p-NA, Boc-Gly-Gly-X-Phe-p-NA, Gly-X-Gly-Phe-p-NA·TFA, and Boc-Gly-X-Gly-Phe-p-NA, with X = ΔZPhe and ΔAla, were studied with NMR in DMSO and CDCl3-DMSO, and with CD in MeOH, MeCN, and TFE. The NMR spectra measured in DMSO suggest that peptides with the ΔPhe residue next to Phe are folded whereas peptides with Gly between ΔPhe and Phe are less ordered. NMR spectra of ΔAla-containing peptides indicate that these peptides are flexible and their conformational equilibria are populated by many different conformations. The CD spectra show that conformational properties of the peptides studied are distinctly influenced by a mutual…