Conformational studies of α-amino acids oligo- and polypeptides

Both oligo- and polypeptides as well as proteins are intrinsically dynamic macromolecules of a remarkable degree of flexibility. Therefore, exploring the accessible conformational space, E=E(fi[1], psi[1], fi[2], psi[2],…,fi[n], psi[n]), of the appropriate building blocks (amino acid derivatives) is of great importance. Multidimensional conformational analysis (MDCA) is a powerful tool applicable at different levels of theory (RHF, DFT, MP2, CCSD, etc.) routinely applied in our group. Around the millennium we have explored the conformational preferences of several aromatic (Phe, His, etc.) and aliphatic (Val, Pro, Ser, Cys, Asp, Ala, Gly, etc.) amino acid incorporating model peptides as well as studied the accessible geometries of polar residues (Ser, Asp, Asn, Gln) and selective derivatives (e.g. Ser-O-Glc, selenoCys). Moreover, we have studied the energetics of selected secondary structural elements, namely the α- and 3/10-helices, β-turns, and β-sheets, etc.. Furthermore, the protonation and deprotonation of side chains during biocatalysis, oligo- and polymerization as well as 3D-fold exchange were studied and beside structure and energetics, PA and pKa values were also determined.

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