The backbone structure of the major cold-shock protein CS7.4 of Escherichia coli in solution includes extensive beta-sheet structure.
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.[1]References
- The backbone structure of the major cold-shock protein CS7.4 of Escherichia coli in solution includes extensive beta-sheet structure. Chatterjee, S., Jiang, W., Emerson, S.D., Inouye, M. J. Biochem. (1993) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
