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 β-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

IACOVINO, Rosa;
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 β-bend conformations located at the -L-Pip-Aib-, -Aib-Gly-, and -L-Leu-Aib- sequences, respectively.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11591/218353
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 1
  • ???jsp.display-item.citation.isi??? 1
social impact