title: β-Turn structure in glycinylphenylalanine dipeptide based N-amidothioureas.
abstract: Transforming the C-terminal amide of a glycinylphenylalanine dipeptide into N-amidothiourea affords a β-turn structure in the formed dipeptide based N-amidothioureas, which can be readily identified by an induced CD signal from the achiral phenylthiourea chromophore.
authors: Department of Chemistry, College of Chemistry and Chemical Engineering, MOE Key Laboratory of Analytical Sciences, and Collaborative Innovation Center of Chemistry for Energy Materials (iChEM), Xiamen University, Xiamen 361005, China. ybjiang@xmu.edu.cn.
authors: Xiao-Sheng
authors: XS
authors: Yan
authors: Kun
authors: K
authors: Wu
authors: Yuan
authors: Y
authors: Yuan
authors: Ying
authors: Y
authors: Zhan
authors: Jin-He
authors: JH
authors: Wang
authors: Zhao
authors: Z
authors: Li
authors: Yun-Bao
authors: YB
authors: Jiang
mesh_terms: D000577:Amides / Q000737:chemistry; D002942:Circular Dichroism; D004151:Dipeptides / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D017433:Protein Structure, Secondary; D013890:Thiourea / Q000737:chemistry*
chemical_list: D000577:Amides; D004151:Dipeptides; D013890:Thiourea