Design and characterization of a homodimeric antiparallel coiled coil.
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.
Gurnon
Daniel G
DG
Department of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405-7102, USA.
Whitaker
Jennifer A
JA
Oakley
Martha G
MG
D002942:Circular Dichroism; D019281:Dimerization; D057927:Hydrophobic and Hydrophilic Interactions; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D011506:Proteins