期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 132, 期 23, 页码 7868-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja103233a
关键词
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资金
- NSF [CHE-0848847]
- NIH
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [848847] Funding Source: National Science Foundation
We report the first high-resolution structural data for the beta/gamma-peptide 13-helix (i,i+3 C=O center dot center dot center dot H-N H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of beta- and gamma-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies suggested that beta/gamma-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized beta- and gamma-residues, which strongly promote 13-helical folding by the 1:1 beta/gamma backbone.
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