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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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K. Satheeshkumar (2002) studied this question.
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