The Tryptic Peptides of the Coat Protein from Wild Type Cowpea Chlorotic Mottle Virus
نویسندگان
چکیده
منابع مشابه
The structure of cucumber mosaic virus and comparison to cowpea chlorotic mottle virus.
The structure of cucumber mosaic virus (CMV; strain Fny) has been determined to a 3.2-A resolution using X-ray crystallography. Despite the fact that CMV has only 19% capsid protein sequence identity (34% similarity) to cowpea chlorotic mottle virus (CCMV), the core structures of these two members of the Bromoviridae family are highly homologous. As suggested by a previous low-resolution struct...
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The four components of the genome of cowpea chlorotic mottle virus have been prepared in a highly active and highly purified state by a method based on their resolution by polyacrylamide gel electrophoresis. Activity and purity have been confirmed by gel electrophoresis under denaturing and non-denaturing conditions, infectivity tests on whole plants, translation in an mRNA dependent rabbit ret...
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We present the modification of the outer protein shell of cowpea chlorotic mottle virus (CCMV) with linear and strained alkyne groups. These functionalized protein capsids constitute valuable platforms for post-functionalization via click chemistry. After modification, the integrity of the capsid and the reversible disassembly behavior are preserved.
متن کاملStructural rigidity in the capsid assembly of cowpea chlorotic mottle virus
The cowpea chlorotic mottle virus (CCMV) has a protein cage, or capsid, which encloses its genetic material. The structure of the capsid consists of 180 copies of a single protein that self-assemble inside a cell to form a complete capsid with icosahedral symmetry. The icosahedral surface can be naturally divided into pentagonal and hexagonal faces, and the formation of either of these faces ha...
متن کاملMolecular modeling of the RNA binding N-terminal part of cowpea chlorotic mottle virus coat protein in solution with phosphate ions.
The RNA-binding N-terminal arm of the coat protein of cowpea chlorotic mottle virus has been studied with five molecular dynamics simulations of 2.0 ns each. This 25-residue peptide (pep25) is highly charged: it contains six Arg and three Lys residues. An alpha-helical fraction of the sequence is stabilized in vitro by salts. The interaction of monophosphate (Pi) ions with pep25 was studied, an...
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ژورنال
عنوان ژورنال: Journal of General Virology
سال: 1979
ISSN: 0022-1317,1465-2099
DOI: 10.1099/0022-1317-43-1-143