Design and Characterization of a Homodimeric Antiparallel Coiled Coil
- 1 June 2003
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 125 (25) , 7518-7519
- https://doi.org/10.1021/ja0357590
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.Keywords
This publication has 24 references indexed in Scilit:
- Evaluation of the energetic contribution of interhelical coulombic interactions for coiled coil helix orientation specificityJournal of Molecular Biology, 2001
- Mechanisms of Viral Membrane Fusion and Its InhibitionAnnual Review of Biochemistry, 2001
- Coiled coils: a highly versatile protein folding motifTrends in Cell Biology, 2001
- De Novo Design and Structural Characterization of Proteins and MetalloproteinsAnnual Review of Biochemistry, 1999
- The role of position a in determining the stability and oligomerization state of α‐helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteinsProtein Science, 1999
- Coiled coils: new structures and new functionsTrends in Biochemical Sciences, 1996
- The Alacoil: A very tight, antiparallel coiled‐coil of helicesProtein Science, 1995
- A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper MutantsScience, 1993
- Peptide ‘Velcro’: Design of a heterodimeric coiled coilCurrent Biology, 1993
- X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled CoilScience, 1991