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- W2079072752 abstract "The coat protein of f2 bacteriophage has been modified in an attempt to determine the effects of changes in primary structure on the ability of this protein monomer to form shells in vitro. Cleavage by cyanogen bromide results in loss of ability to form shells; however, the fragments produced were active in inhibiting shell formation by unmodified protein. Reactions aimed at sulfhydryl and methionine residues resulted in precipitation of the protein monomer and attendant loss of ability to form shells. Arginine residues were reacted with phenylglyoxal hydrate: in the monomer, this prevented shell formation; although phage disintegrated upon treatment with reagent, the empty protein shells remained intact. Cleavage of the carboxyl-terminal tyrosine by carboxypeptidase produced a modified protein which was incapable of forming shells, but which prevented intact monomers from achieving the conformation necessary for shell formation. Shells and phage treated with carboxypeptidase did not release the carboxylterminal tyrosine residue." @default.
- W2079072752 created "2016-06-24" @default.
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- W2079072752 date "1972-03-01" @default.
- W2079072752 modified "2023-09-27" @default.
- W2079072752 title "Effects of chemical modification of f2 viral coat protein on its shell-forming activity" @default.
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- W2079072752 doi "https://doi.org/10.1016/0022-2836(72)90488-3" @default.
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