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- W1994092425 abstract "The near-u.v. circular dichroism of papaya mosaic virus coat protein is dominated by intrasubunit interactions involving tryptophan and, to a much lesser extent, phenylalanine. The conformations of the 14 S protein discs at pH 4.0, pH 6.0 and pH 8.0 are judged to be similar by circular dichroism. At pH 8.0, however, the conformation of the protein is influenced by the extent of aggregation, which is reflected in the intensity, but not the shape, of the circular dichroism spectrum. The increase in intensity level that accompanies aggregation at pH 8.0 mainly appears to reflect modifications of tryptophanyl interactions. On the other hand, no spectral changes result when discs polymerize to form helical tubes at pH 4.0, indicating that a major conformational change is not requisite for helix formation. The above results are interpreted in view of the various protein and virus assembly reactions in which papaya mosaic virus coat protein participates. Denaturation of the coat protein results in quenching of optical activity in the near-u.v. region, and also in marked changes in the u.v. spectrum of the protein. These results indicate that the majority of the tryptophan and tyrosine residues are buried within a hydrophobic environment in the undenatured protein." @default.
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- W1994092425 date "1981-04-01" @default.
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- W1994092425 title "Circular dichroism studies of papaya mosaic virus coat protein and its polymers" @default.
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- W1994092425 doi "https://doi.org/10.1016/0022-2836(81)90444-7" @default.
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