In this paper we present a redesign strategy for the development of uniquely folded polypeptide motifs of less than 40 residues. These mini proteins are based on natural target domains, including the zinc finger domains (BBA motif)\* and the disulfide-rich snake and scorpion toxins (BBB motif). Thes
β¦ LIBER β¦
A CD strategy for the study of polypeptide folding/unfolding
β Scribed by SILIGARDI, GIULIANO ;DRAKE, ALEX F. ;MASCAGNI, PAOLO ;ROWLANDS, DAVID J. ;BROWN, FRED ;GIBBONS, WILLIAM A.
- Book ID
- 115099275
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 663 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0367-8377
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## Abstract Irrespective of the constituent protein, all amyloid fibrils show similar morphology in the electron microscope and xβray diffraction patterns characteristic of a βcrossβΞ²β structure, with extended Ξ²βstrands perpendicular to the fibril's long axis. Little is known about the amount or ty