1.
Eur Respir J
; 40(1): 269-70, 2012 Jul.
Artigo
em Inglês
| MEDLINE
| ID: mdl-22753837
2.
J Am Chem Soc
; 133(12): 4246-9, 2011 Mar 30.
Artigo
em Inglês
| MEDLINE
| ID: mdl-21370877
RESUMO
The invention of new strategies for the design of protein-mimetic oligomers that manifest the folding encoded in natural amino acid sequences is a significant challenge. In contrast to the α-helix, mimicry of protein ß-sheets is less understood. We report here the aqueous folding behavior of a prototype α-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different ß-amino acid monomers. Our results provide a folding propensity scale for ß-residues in a protein ß-sheet context as well as high-resolution structures of several mixed-backbone α/ß-peptide hairpins in water.