Design strategies for the construction of independently folded polypeptide motifs.
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). These motifs are designed to act as the molecular framework for the construction of novel functional polypeptides. We will explore the structural determinants of the folded BBA motif, inspired by the zinc finger peptides, in relation to the redesign process.
Imperiali
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Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA.
Ottesen
J J
JJ
D000595:Amino Acid Sequence; D001704:Biopolymers / Q000737:chemistry; D015195:Drug Design; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D016335:Zinc Fingers
D001704:Biopolymers; D010455:Peptides