Scientific article

Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae

Published inFEBS letters, vol. 414, no. 3, p. 590-594
Publication date1997

A new ice nucleation gene from Pseudomonas syringae was isolated and overexpressed as a fully active protein in Escherichia coli in order to gain experimental data about the structure of ice nucleation proteins. No evidence of a signal sequence or secondary glycosylation was found. Differences in the extent of aggregation were shown to modulate the ice nucleation activity. The circular dichroism spectrum of the purified protein indicated the presence of beta-sheet structure. This finding supports a recently proposed hypothetical model for the structure of ice nucleation proteins, which provides a plausible explanation for their aggregation tendency.

  • Bacterial ice nucleation
  • InaV sequence
  • Protein aggregation
  • ß-strand
  • Pseudomonas syringae
Affiliation Not a UNIGE publication
Citation (ISO format)
SCHMID, Daniel et al. Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae. In: FEBS letters, 1997, vol. 414, n° 3, p. 590–594. doi: 10.1016/s0014-5793(97)01079-x
Main files (1)
Article (Published version)
ISSN of the journal0014-5793

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