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PMID: 275841 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Amino-terminal sequence analysis of the structural proteins of Sindbis virus.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 6 ·1978-06-00 ·Pages 2722-6

Bell JR, Hunkapiller MW, Hood LE, Strauss JH

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 NH2-terminal sequences of about 50 residues were determined for each of the two membrane glycoproteins. In both cases the NH2 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 alpha-amino group. This is consistent with other observations that viral proteins derived from the NH2 terminus of precursor molecules are often blocked.

MeSH Terms
Amino Acid Sequence Autoanalysis Glycoproteins Membrane Proteins Microchemistry Sindbis Virus Viral Proteins
Chemicals
Glycoproteins Membrane Proteins Viral Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Bell J R
Hunkapiller M W
Hood L E
Strauss J H
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23 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.75.6.2722
Published
1978-06-00
Pages
2722-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC392635
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.6.2722 PMC Full Text View journal details
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