Tryptophan zippers: stable, monomeric beta -hairpins.
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ABSTRACT:
SUBMITTER: Cochran AG
PROVIDER: S-EPMC33255 | biostudies-literature | 2001 May
REPOSITORIES: biostudies-literature
Publications
Tryptophan zippers: stable, monomeric beta -hairpins.
Cochran A G AG Skelton N J NJ Starovasnik M A MA
Proceedings of the National Academy of Sciences of the United States of America 20010501 10
A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the beta-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 beta-hairpins and even those of some larger designed proteins. NMR structures of three of the trpzip p ...[more]
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