In the transition from secondary to tertiary structure in peptides and proteins, turns take a special role. They are the hinges that arrange the periodic secondary structure elements (helices and strands) to the native fold. It is a known effect that Li+ alters peptide backbone structure, and we investigate this effect on the structure and dynamics of turns for model peptides Ac-Ala-Ala-Pro-Ala-NMe (AAPA) and Ac-Ala-Asp-Pro-Ala-NMe (ADPA) by theoretical conformational predictions and experimental vibrational spectroscopy.
Local Conformational Preferences of Peptides Near Attached Cations: Structure Determination by First-Principles Theory and IR-Spectroscopy
Baldauf, C.*; Pagel, K.; Warnke, S.; von Helden, G.; Meijer, G.; Koksch, B.; Blum, V.; Scheffler, M.