The Backbone Structure of the Major Cold-Shock Protein CS7.4 of Escherichia coli in Solution Includes Extensive β-Sheet Structure1
| Autor: | Weining Jiang, Masayori Inouye, S. D. Emerson, Sukalyan Chatterjee |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Stereochemistry Beta sheet General Medicine Nuclear magnetic resonance spectroscopy Cold-shock domain Biology medicine.disease_cause Biochemistry Amino acid Protein structure chemistry medicine Molecular Biology Escherichia coli Protein secondary structure |
| Zdroj: | The Journal of Biochemistry. 114:663-669 |
| ISSN: | 1756-2651 0021-924X |
| DOI: | 10.1093/oxfordjournals.jbchem.a124234 |
| Popis: | CS7.4 is the major cold-shock protein specifically expressed to a level as high as 13% of the total cellular protein within the first hour when Escherichia coli cell culture is shifted from 37 to 15 degrees C [Goldstein et al. (1990) Proc. Natl. Acad. Sci. USA 87, 283-287]. It consists of 70 amino acid residues with a very high content of aromatic residues. CS7.4 was overproduced and purified to homogeneity. Its secondary structure was analyzed by examining circular dichroism at both the far and near-UV regions; the results suggest that the protein is largely beta-sheet in conformation. The predominance of beta-sheet structure in the protein was confirmed by using Fourier-transform infrared spectroscopy. A folded compact conformation was also verified by fluorescence emission spectroscopy. We evaluated Tm, delta H, and delta S from the thermal denaturation profile of the protein. Unusual spectral features observed in the far-UV region are attributed to the high content of aromatic residues. The protein is relatively small and contains no disulfide bonds. However, it is surprisingly stable to heat denaturation. |
| Databáze: | OpenAIRE |
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