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Amino acid sequence of the coat protein subunit in satellite tobacco necrosis virus
dc.contributor.authorHenriksson, Dag M.en_US
dc.contributor.authorTanis, Robert J.en_US
dc.contributor.authorTashian, Richard E.en_US
dc.contributor.authorNyman, P. O.en_US
dc.date.accessioned2006-04-07T18:01:03Z
dc.date.available2006-04-07T18:01:03Z
dc.date.issued1981-10-15en_US
dc.identifier.citationHenriksson, D., Tanis, R. J., Tashian, R. E., Nyman, P. O. (1981/10/15)."Amino acid sequence of the coat protein subunit in satellite tobacco necrosis virus." Journal of Molecular Biology 152(1): 171-179. <http://hdl.handle.net/2027.42/24232>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WK7-4DM0X82-R/2/69ba91517502c2e634da248ff74a3ddben_US
dc.identifier.urihttps://hdl.handle.net/2027.42/24232
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=7338907&dopt=citationen_US
dc.description.abstractThe primary structure of the coat protein subunit in satellite tobacco necrosis virus has been investigated. The results obtained are consistent with and support the proposal for the amino acid sequence made from the nucleotide sequence of RNA (Ysebaert et al., 1980). This would imply that no intervening sequences of RNA occur in the cistron for the satellite tobacco necrosis virus coat protein. The polypeptide chain of the protein consists of 195 amino acid residues. It contains one sulfhydryl group but no disulfide bridges. The distribution of various kinds of amino acid residues along the chain is markedly uneven.en_US
dc.format.extent664308 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleAmino acid sequence of the coat protein subunit in satellite tobacco necrosis virusen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Human Genetics University of Michigan Medical School, Ann Arbor, Mich. 48109, U.S.A.; Department of Biochemistry and Biophysics University of Göteborg and Chalmers Institute of Technology S-412 96, Gothenburg, Swedenen_US
dc.contributor.affiliationumDepartment of Human Genetics University of Michigan Medical School, Ann Arbor, Mich. 48109, U.S.A.en_US
dc.contributor.affiliationumDepartment of Human Genetics University of Michigan Medical School, Ann Arbor, Mich. 48109, U.S.A.en_US
dc.contributor.affiliationotherDepartment of Biochemistry and Biophysics University of Göteborg and Chalmers Institute of Technology S-412 96, Gothenburg, Swedenen_US
dc.identifier.pmid7338907en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/24232/1/0000492.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0022-2836(81)90101-7en_US
dc.identifier.sourceJournal of Molecular Biologyen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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