| Literature DB >> 16248623 |
Eleonora Cerasoli1, Belinda K Sharpe, Derek N Woolfson.
Abstract
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 alpha-helical coiled-coil trimer and zinc-bound monomer. Solution-phase spectroscopic, sedimentation, and binding studies confirmed the key aspects of the design. Both forms of the peptide were cooperatively folded, and the switch between them was reversible. This design process potentially presents a novel route to peptide-based biosensors.Entities:
Mesh:
Substances:
Year: 2005 PMID: 16248623 DOI: 10.1021/ja0543604
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419