Dipeptides are amino acids blocked with an acetyl and an N-methyl group. The amino acids in dipeptides have structural properties similar to amino acid residues in proteins; this is why structures of dipeptides are important for understanding structures of proteins. We have determined the dipeptide structures of 19 basic amino acids in a water solution. Using spectroscopic methods, we have demonstrated the presence of three conformations of dipeptides in water: the PII, ß, and the ?R. The proportion of the ?R conformation in all dipeptides is surprisingly low (( 10%).
B.04 Guest lecture
COBISS.SI-ID: 4501018A LC-MS assay for monitoring the enzyme activity of UDP-N-acetylmuramyl-L-alanine:D-glutamate ligase (MurD) was developed for quantitative detection of the reaction product UDP-MurNac-L-Ala-D-Glu. The method is a valuable orthogonal (secondary) assay to the primary high throughput fluorescence assay screening and is fully compatible with the components from the primary assay and enables the analysis of the same samples. Proteins are removed by ultrafiltration.
F.21 Development of new health/diagnostic methods/procedures
COBISS.SI-ID: 99999999We developed a new method based on ATR and difference spectroscopy for determination of various types of celluloses. Difference spectroscopy enables to observe small changes in vibrational spectra even in the presence of auxiliary substances in final formulation of the drug.
D.01 Chairing over/coordinating (international and national) projects
COBISS.SI-ID: 99999999We applied ATR spectroscopy and PLS1 chemometric method for quantitative determination of the presence of three most common polysaccharide isomers. The method based on the assumption that the input samples are pure composed of solely one isomer.
D.01 Chairing over/coordinating (international and national) projects
COBISS.SI-ID: 99999999Simona Golič Grdadolnik and Jože Grdadolnik are mentors of four graduate stidents.
D.09 Tutoring for postgraduate students
COBISS.SI-ID: 99999999