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- W1569600411 abstract "An analog of the C-terminal tricosapeptide of secretin, with aspartic acid replacing glutamic acid in position 9 and lysine substituted for arginine in position 21, was prepared. The synthesis was carried out in solution by stepwise chain lengthening with the application of the in situ technique. The ord-cd spectra of this new analog closely resemble the spectra of the tricosapeptide with the unaltered secretin sequence and of the analog in which only arginine-21 was replaced by lysine and of secretin itself. The incorporation of aspartic acid instead of glutamic acid-9 resulted in an N-terminal sequence that has a consïderably reduced probability of assuming a helical conformation. The observation that the helix content remained unchanged adds support to a model of secretin in which the helical stretch is near the C-terminus. The role of an acidic residue in position 9 is also discussed." @default.
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- W1569600411 date "1976-09-01" @default.
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- W1569600411 title "Studies on the conformation of secretin" @default.
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- W1569600411 doi "https://doi.org/10.1016/0045-2068(76)90036-5" @default.
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