Published June 1978
| Published
Journal Article
Open
Amino-terminal sequence analysis of the structural proteins of Sindbis virus
Abstract
The structural proteins of Sindbis virus, an enveloped virus which belongs to the Togavirus family, have been subjected to automated Edman degradation using improved techniques. Extensive NHrterminal sequences of about 50 residues were determined for each of the two membrane glycoproteins. In both cases the NH_2 terminus of the molecule was found to be similar in composition to typical water-soluble proteins. The viral capsid protein was found to have a blocked a-amino group. This is consistent with other observations that viral proteins derived from the NH_2 terminus of precursor molecules are often blocked.
Additional Information
© 1978 National Academy of Sciences. Communicated by N. H. Horowitz, April 7, 1978. The preliminary sequence data obtained by using the solid-phase instrument were obtained by Dr. W. J. Dreyer and his colleagues and we express our gratitude to him for this work. Edith M. Lenches and Mary S. Martin provided expert technical assistance in the growth of the virus and its purification. This work was supported by Grants GM 06965 and AI110793 from the National Institutes of Health and by Grant PCM 77-26728 from the National Science Foundation.Attached Files
Published - PNAS-1978-Bell-2722-6.pdf
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PNAS-1978-Bell-2722-6.pdf
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Additional details
- PMCID
- PMC392635
- Eprint ID
- 58799
- Resolver ID
- CaltechAUTHORS:20150707-153924494
- GM 06965
- NIH
- AI 110793
- NIH
- PCM 77-26728
- NSF
- Created
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2015-07-08Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field