Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 130, Issue 25, Pages 7839-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja802042c
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Funding
- NIGMS NIH HHS [R01 GM061238-06, R01 GM061238-02, GM61238, R01 GM061238-07, R01 GM061238-09, R01 GM061238, R01 GM061238-05, R01 GM061238-08, R01 GM061238-01, R01 GM061238-04, R01 GM061238-03] Funding Source: Medline
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We report the development of diacid units that promote formation of a two-stranded parallel beta-sheet secondary structure between peptide segments attached via their N-termini. These linker units are formed by attaching glycine to one carboxyl group of cis-1,2-cyclohexanedicarboxylic acid (CHDA). Parallel sheet formation in water is observed when L-residue strands are attached to the CHDA-Gly unit with either of the two absolute configurations.
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