A. Mascioni, C. Karim, J. Zamoon, D. D. Thomas and G. Veglia, “Solid-State NMR and Rigid Body Molecular Dynamics to Determine Domain Orientations of Mono-meric Phospholamban,” Journal of the American Chemi-cal Society, Vol. 124, No. 32, 2002, pp. 9392-9393. doi:10.1021/ja026507m

has been cited by the following article:

• TITLE: Improved Solid-Phase Peptide Synthesis of Wild-Type and Phosphorylated Phospholamban Using a Pseudoproline Dipeptide

  AUTHORS: Shadi Abu-Baker, Gary A. Lorigan

  KEYWORDS: Solid-State Peptide Synthesis; Pseudoproline Dipeptide; Phospholamban

  JOURNAL NAME: Open Journal of Synthesis Theory and Applications, Vol.1 No.2, July 30, 2012

  ABSTRACT: In this study, we report that the insertion of a pseudoproline dipeptide for the solid-phase peptide synthesis of wild-type Phospholamban protein (WT-PLB) has two important advantages. First, it disrupts the formation of different secondary structures, which is responsible for poor couplings during the preparation of highly aggregated sequences. Second, it enhances the purities and solubility of crude products leading to easier HPLC purification.