期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 131, 期 29, 页码 9860-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja8099294
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资金
- NCI NIH HHS [F32 CA119875, CA119875] Funding Source: Medline
- NIGMS NIH HHS [R01 GM061238-06, R01 GM061238-04, GM61238, R01 GM061238-01, R01 GM061238-09, R01 GM061238-10, R01 GM061238-08, R01 GM061238-02, R01 GM061238-07, R01 GM061238-05, R01 GM061238, R01 GM061238-03] Funding Source: Medline
Helix bundles are among the most widely studied tertiary and quaternary structural motifs in proteins. Here we present the crystal structure of an alpha/beta-peptide foldamer that adopts a tetrameric helix-bundle quaternary structure with a hydrophobic core composed solely of beta-amino acids. The structure displays features that are unprecedented among all known helix bundles composed of either a-peptides or peptidic foldamers. The tetramer is characterized by an asymmetry of interaction between neighboring hetices, and the side-chain packing within the hydrophobic core differs fundamentally from the knobs-into-holes arrangement typical of most helix bundles.
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