ZiCo:  A Peptide Designed to Switch Folded State upon Binding Zinc

• Published in: Journal of the American Chemical Society Vol. 127; no. 43; pp. 15008 - 15009
• Main Authors: Cerasoli, Eleonora, Sharpe, Belinda K, Woolfson, Derek N
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 02.11.2005
• Subjects: Binding Sites; Biological and medical sciences; Chlorides - chemistry; Chlorides - metabolism; Circular Dichroism; Conformational dynamics in molecular biology; Edetic Acid - chemistry; Edetic Acid - metabolism; Fundamental and applied biological sciences. Psychology; Molecular biophysics; Peptides - chemistry; Peptides - metabolism; Protein Folding; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Temperature; Zinc - chemistry; Zinc - metabolism; Zinc Compounds - chemistry; Zinc Compounds - metabolism; Amphipathic compound; Helix coil transition; Peptides; Zinc finger structure; Conformational dynamics; Circular dichroism spectrometry; Molecular interaction; NMR spectrometry; Conformational changes; Conformational transition

We describe a novel approach to the design of a metal-triggered conformational switch. Specifically, two distinct protein-folding motifs were merged into one polypeptide sequence. The target structures were an α-helical coiled-coil trimer and zinc-bound monomer. Solution-phase spectroscopic, sedimen...