期刊
CHEMICAL COMMUNICATIONS
卷 -, 期 19, 页码 2244-2245出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/b206886a
关键词
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A hydrophobic pentadecapeptide, AGAAAA-GAVVGGLGG (1), part of the prion sequence PrP (106-127), on fresh aqueous dissolution takes a mixture of random and sheet conformations which forms a stable monolayer with a high beta-sheet content when compressed at the air-water interface. This also develops into a kinetically stabilized beta-sheet structure on sonication.
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