Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae
| Autor: | Jean-Richard Neeser, Alfred Jann, Daniel Schmid, Guido Capitani, David Pridmore, Roberto Battistutta |
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| Rok vydání: | 1997 |
| Předmět: |
Signal peptide
Circular dichroism Cytoplasm Glycosylation Protein Conformation Detergents Immunoblotting Molecular Sequence Data Bacterial ice nucleation Biophysics Pseudomonas syringae Protein aggregation Biology medicine.disease_cause Biochemistry chemistry.chemical_compound Structural Biology Pseudomonas Genetics medicine Escherichia coli ß-strand Cloning Molecular β-strand InaV sequence inaV sequence Molecular Biology Gene PURIFICATION NUCLEI Temperature Cell Biology GENE Recombinant Proteins Cell Compartmentation MODEL Crystallography chemistry Ice nucleus Bacterial Outer Membrane Proteins Subcellular Fractions |
| Zdroj: | FEBS Letters, Vol. 414, No 3 (1997) pp. 590-594 |
| ISSN: | 0014-5793 |
| Popis: | 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 β-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. |
| Databáze: | OpenAIRE |
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