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De novo design of heterotrimeric coiled coils
Author(s) -
Lombardi Angela,
Bryson James W.,
DeGrado William F.
Publication year - 1996
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1996)40:5<495::aid-bip7>3.0.co;2-r
Subject(s) - heterotrimeric g protein , chemistry , helix bundle , antiparallel (mathematics) , protein design , coiled coil , circular dichroism , sedimentation equilibrium , biophysics , crystallography , helix (gastropod) , protein structure , ultracentrifuge , biochemistry , g protein , signal transduction , biology , physics , quantum mechanics , magnetic field , ecology , snail
The three‐helix bundle is a common structural motif among natural proteins. It has been observed in numerous important proteins, such as fibrinogen, laminin, spectrin, dystrofin, hemagglutinin, and mannose binding proteins. The three‐helix bundle is a simple structure in which three α‐helices pack against each other, with a slight left‐handed twist. Because of its simplicity relative to other structural motifs, the three‐helix bundle can be conveniently used both to clarify the forces responsible for the protein folding and stability, and for the design of novel proteins. In this paper we describe the design, synthesis, and characterization of three peptides that self‐assemble into antiparallel, heterotrimeric coiled coils. The experimental results, obtained from CD spectroscopy and ultracentrifugation equilibrium sedimentation, indicate that the mixture of the three peptides preferentially forms heterotrimers; moreover, these aggregates represent attractive systems for combinatorial design of libraries of pseudo C 3 symmetric ligands or binding sites. © 1997 John Wiley & Sons, Inc. Biopoly 40: 495–504, 1996