Selection of a buried salt bridge by phage display.
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.
Department of Biology, Chemistry and Pharmacy-Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany.
Toni
T
Vagt
Christian
C
Jäckel
Sergey
S
Samsonov
M
M
Teresa Pisabarro
Beate
B
Koksch
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D019151:Peptide Library; D011485:Protein Binding; D015202:Protein Engineering; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D019151:Peptide Library