Conformational analysis of Cystein e side chain for HC O-L-Cys- L-Ala-NH۲ protected dipe ptide. A DFT study

The aim of this study is to investigate the role of Cysteine side chain on the s tability of L-Cys–L-A la protected dipeptide(s ee Fig ۱). T he ۲۰ naturally occurring amino acids 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.