Environment-controlled interchromophore charge transfer transitions in dipeptides probed by UV absorption and electronic circular dichroism spectroscopy

Article Abstract:

Charge transfer (CT) transitions between the C-terminal carboxylate and peptide group are investigated for alanyl-X and X-alanine dipeptides by far-ultraviolet (UV) absorption and electronic circular dichroism (ECD) spectroscopy (where X represented different amino acid residues). The ECD technique is also used as a convenient tool to detect the influence of the negatively charged side chains on the pK value and the structure of the C-terminal carboxylate group.

Charge transfer, Chemical properties, Atomic properties, Carboxyl compounds

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Different conformers and protonation states of dipeptides probed by polarized Raman, UV-resonance Raman, and FTIR spectroscopy

Article Abstract:

A study was conducted relating to research on the peptide group-containing simple molecule N-methylacetimide as a model for probing the amide linkage in proteins and peptides. The study investigated the entire frequency region between 800 and 1800 cm-1 of glicylglycine (DGL: diglycine) and N-acetylglycine in H20 and D2O. using various spectroscopic methods. Experimental methodology, findings and conclusions are discussed.

Research, Case studies, Peptides, Proteins, Spectrum analysis, Spectroscopy, Molecules, Amides, Molecular spectra

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Conformational analysis of XA and AX dipeptides in water by electronic circular dichroism and [.sup.1.H]NMR spectroscopy

Article Abstract:

The temperature dependent electronic circular dichroism (ECD) spectra of AX, XA, and XG dipeptides in D2O were measured. The spectra of all XA and AX peptides indicate a substantial population of the polyproline II (PPII) conformation while the ECD spectra of LG, KG, PG and AG were found to be quantitatively different from the alanine based dipeptides.

Usage, Nuclear magnetic resonance spectroscopy, Spectra, Alanine

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