Conformational studies of α-amino acids and peptides


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Proteins and peptides are dynamic compounds with a remarkable degree of flexibility. Therefore, the exploration of the accessible conformations of peptide building blocks is of great importance. Muldidimensional conformational analysis (MDCA) is a powerfool tool that can be used for all available levels of molecular calculations, including quantum chemistry, used in our group. We have explored the conformational preferences of several aromatic (Phe, His) and aliphatic amino acid residues (Val, Pro, Ser, Cys, Asp, Ala, Gly) amino acid incorporating model peptides as well as as studied the accessible geometries of polar residues (Ser, Asp, O-GlcSer, selenoCys). Moreover, we are investigating the energetics of seconadry structure elements, namely α- and 310-helices, β-turns, and β-sheets at differennt levels of theory.


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