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Title: Helix Bundle Quaternary Structure from [alpha]/[beta]-Peptide Foldamers

Journal Article · · J. Am. Chem. Soc.
DOI:https://doi.org/10.1021/ja070396f· OSTI ID:1007654

The function of a protein generally depends on adoption of a specific folding pattern, which in turn is determined by the side chain sequence along the polypeptide backbone. Here we show that the sequence-encoded structural information in peptides derived from yeast transcriptional activator GCN4 can be used to prepare hybrid {alpha}/{beta}-peptide foldamers that adopt helix bundle quaternary structures. Crystal structures of two hybrid {alpha}/{beta}-peptides are reported along with detailed structural comparison to {alpha}-peptides of analogous side chain sequence. There is considerable homology between {alpha}- and {alpha}/{beta}-peptides at the level of helical secondary structure, with modest but significant differences in the association geometry of helices in the quaternary structure.

Research Organization:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
USDOE
OSTI ID:
1007654
Journal Information:
J. Am. Chem. Soc., Vol. 129, Issue (14) ; 04, 2007; ISSN 0002-7863
Country of Publication:
United States
Language:
ENGLISH

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