Tryptophan zippers: Stable, monomeric β-hairpins


Autoria(s): Cochran, Andrea G.; Skelton, Nicholas J.; Starovasnik, Melissa A.
Data(s)

08/05/2001

01/05/2001

Resumo

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.

Identificador

/pmc/articles/PMC33255/

/pubmed/11331745

http://dx.doi.org/10.1073/pnas.091100898

Idioma(s)

en

Publicador

The National Academy of Sciences

Direitos

Copyright © 2001, The National Academy of Sciences

Palavras-Chave #Biological Sciences
Tipo

Text