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Title: Selection of a buried salt bridge by phage display. Author: Vagt T, Jäckel C, Samsonov S, Teresa Pisabarro M, Koksch B. Journal: Bioorg Med Chem Lett; 2009 Jul 15; 19(14):3924-7. PubMed ID: 19369078. Abstract: The alpha-helical coiled coil is a valuable folding motif for protein design and engineering. By means of phage display technology, we selected a capable binding partner for one strand of a coiled coil bearing a charged amino acid in a central hydrophobic core position. This procedure resulted in a novel coiled coil pair featuring an opposed Glu-Lys pair arranged staggered within the hydrophobic core of a coiled coil structure. Structural investigation of the selected coiled coil dimer by CD spectroscopy and MD simulations suggest that a buried salt bridge within the hydrophobic core enables the specific dimerization of two peptides.[Abstract] [Full Text] [Related] [New Search]