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The repeat distances of 4.7 and 6.9 Å, which have been observed previously in crystalline β-sheet structures, can be used to estimate the area per molecule. For example, (4 x 4.7 x 6.9) Å = 129.7 Å for an eight-residue peptide; see ref. [15].
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46
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31444446162
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In aqueous solution the acetylated octapeptide 3 showed a random-coil conformation.
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47
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2 solution subphases showed that the interstrand distance remained constant upon compression. The strand length, however, appeared to have an elastic behavior, as the conformation of the backbone changed upon compression.
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