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- W2044005473 abstract "Structure analysis jointly based on circular dichroism and Chou and Fasman analysis has been performed on a homologous group of 12 squash proteinase inhibitors. The analysis favours a structure incorporating 40–45% helix which is tightly crosslinked by three disulphide bonds. The proposed structure is consistent with the previously published CD and 1H n.m.r. spectra. The amino acid which forms the centre of the interaction between trypsin and the inhibitor, arginine5 or lysine5, is located on the N-terminus of one of the helical segments. The basic residue is orientated away from the rest of the structure and thus is ideally situated for interaction with the confined space of the trypsin active site." @default.
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- W2044005473 date "2009-01-12" @default.
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- W2044005473 title "Structure analysis of trypsin inhibitors isolated from Cucurbitacae seeds. Circular dichroism studies" @default.
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- W2044005473 doi "https://doi.org/10.1111/j.1399-3011.1987.tb03347.x" @default.
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