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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.
Design of a discretely folded mini-protein motif with predominantly beta-structure.,Ottesen JJ, Imperiali B Nat Struct Biol. 2001 Jun;8(6):535-9. PMID:11373623[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Ottesen JJ, Imperiali B. Design of a discretely folded mini-protein motif with predominantly beta-structure. Nat Struct Biol. 2001 Jun;8(6):535-9. PMID:11373623 doi:10.1038/88604
