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J Am Chem Soc. 2003 Jun 25;125(25):7518-9.

Design and characterization of a homodimeric antiparallel coiled coil.

Author information

1
Department of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405-7102, USA.

Abstract

We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications.

PMID:
12812483
DOI:
10.1021/ja0357590
[Indexed for MEDLINE]

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