An X-ray diffraction analysis of the C-terminal, fully blocked pentapeptide segment of the antibiotic efrapeptin C Z-L-Pip-Aib-Gly-L-Leu-Aib-NHMe monohydrate showed that its secondary structure is characterized by three non-helical beta-bend conformations located at the -L-Pip-Aib-, -Aib-Gly-, and -L-Leu-Aib- sequences, respectively.
Crystal-state structure of the C-terminal pentapeptide of the antibiotic efrapeptin C
FORMAGGIO, FERNANDO;TONIOLO, CLAUDIO
1996
Abstract
An X-ray diffraction analysis of the C-terminal, fully blocked pentapeptide segment of the antibiotic efrapeptin C Z-L-Pip-Aib-Gly-L-Leu-Aib-NHMe monohydrate showed that its secondary structure is characterized by three non-helical beta-bend conformations located at the -L-Pip-Aib-, -Aib-Gly-, and -L-Leu-Aib- sequences, respectively.File in questo prodotto:
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