The primary structure of cowpea chlorotic mottle virus coat protein
The amino acid sequence of the coat protein of wild-type cowpea chlorotic mottle virus has been nearly completely determined by direct methods. The sites of amino acid replacements were identified in the coat proteins of an oxidation-sensitive mutant, a temperature-sensitive mutant, and a salt-stabl...
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Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1982-01, Vol.119 (2), p.500-503 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The amino acid sequence of the coat protein of wild-type cowpea chlorotic mottle virus has been nearly completely determined by direct methods. The sites of amino acid replacements were identified in the coat proteins of an oxidation-sensitive mutant, a temperature-sensitive mutant, and a salt-stable mutant. The replacements are a cysteinyl residue for the arginyl residue at position 25 in the oxidation-sensitive mutant, glutamic acid and alanine, respectively, for lysine and valine at positions 21 and 87 in the temperature-sensitive mutant, and arginine for lysine at position 105 in the salt-stable mutant. The substitutions are consistent with point mutations. |
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ISSN: | 0042-6822 1096-0341 |
DOI: | 10.1016/0042-6822(82)90108-8 |