作者: Alexander J. Riemen , Marcey L. Waters
DOI: 10.1021/JA101079Z
关键词:
摘要: Protein post-translational modifications (PTMs) are used in nature as a means of turning on or off myriad biological events. Methylation lysine and phosphorylation serine important PTMs the histone code found to modulate chromatin packing, which turn affects gene expression. The design peptides that fold into secondary structures can help further our understanding complex protein interactions. Here we report Trpswitch peptide sequence folds moderately stable β-hairpin structure aqueous solution show stability be tuned by incorporation dimethyllysine phosphoserine. Dimethylated results an increase stability, while phosphorylated is unstructured at neutral pH. When both incorporated Trpswitch, less observed. This system provides model demonstrate how multiple may work concert against each other inf...