Conformational analysi s of Cysteine side ch ain for HCO-D-Cys-D-Ala-NH۲ pr otected dipeptide. A DFT study

The aim of this study is to investigate the role of Cyst eine side chain on the stability of D-Cys–D-A la protecte d dipeptide( see Fig ۱). T he ۲۰ naturally occurring amino ac ids can occur both in the L-and D-enantiomeri c configuration [۱]. As of yet, the process of protein foldin g is not fully understo od. A typical protein has such a multitude of po ssible confo rmations that it can occupy simpl e counting argument of Levinthal[۲]. Dipeptide models ar e increasingly used in peptide fol ding studies as they of typical triamide conformations[۳] folding has received intense stu dy due to its fundamental importan ce in living organisms, the growin g availability of protein sequences , and the increasing recognition that some d iseases are a result misfolded proteins [۴].

کلیدواژه ها:

Cysteine ، Dipeptide ، Dihedral A ngle ، DFT.