Author:
Cochran Andrea G.,Skelton Nicholas J.,Starovasnik Melissa A.
Abstract
A structural motif, the tryptophan zipper (trpzip), greatly
stabilizes the β-hairpin conformation in short peptides. Peptides (12
or 16 aa in length) with four different turn sequences are monomeric
and fold cooperatively in water, as has been observed previously for
some hairpin peptides. However, the folding free energies of the
trpzips exceed substantially those of all previously reported
β-hairpins and even those of some larger designed proteins. NMR
structures of three of the trpzip peptides reveal exceptionally
well-defined β-hairpin conformations stabilized by cross-strand pairs
of indole rings. The trpzips are the smallest peptides to adopt an
unique tertiary fold without requiring metal binding, unusual amino
acids, or disulfide crosslinks.
Publisher
Proceedings of the National Academy of Sciences
Cited by
673 articles.
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