| Literature DB >> 12812483 |
Daniel G Gurnon1, Jennifer A Whitaker, Martha G Oakley.
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.Entities:
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Year: 2003 PMID: 12812483 DOI: 10.1021/ja0357590
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419