Design of a discretely folded mini-protein motif with predominantly beta-structure.
Here we report the creation of a predominantly beta-structured mini-protein motif. The design target is based on the naturally occurring toxin hand (TH) motifs that are composed of four disulfide bonds and three loops that form a 'hand'. Analysis and subsequent modification of several generations of mini-proteins produced the final 29-residue mini-protein. The structured motif of this new mini-protein provides insight into the compensatory changes that result in the formation of a tightly packed hydrophobic core in a small, globular beta-structure motif. Additionally, this mini-motif represents a new, distinct surface topology for protein design and a valuable, yet compact, model system for the study of beta-sheet structure in water.
Ottesen
J J
JJ
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Imperiali
B
B
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D004220:Disulfides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000378:metabolism; D015202:Protein Engineering; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D014118:Toxins, Biological / Q000737:chemistry; D014461:Ultracentrifugation
D004220:Disulfides; D010455:Peptides; D014118:Toxins, Biological