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- W2129675399 abstract "1. Solvent perturbation difference spectra of N-acetyltyrosine ethyl ester and N-acetyltryptophan-amide due to 20% ethylene glycol, 20% glycerol, 10% polyethylene glycol, and 20% sucrose were obtained in the presence of 100 mM Tris-HC1 (pH 8), 0.6M KC1, and 10 mM MgCl2 at 25°C. 2. Under the same conditions solvent perturbation difference spectra of heavy meromyosin and subfragment-1 were obtained. 3. Fraction of accessible tyrosyl and tryptophanyl residues in each protein was determined using the model compound data. For example, 69% tyrosine and 40% tryptophan in heavy meromyosin, and 66% tyrosine and 47% tryptophan in subfragment-1 were accessible to glycerol in native state. 4. No detectable change in the solvent perturbation difference spectra between the free protein and the complexed protein with ATP was observed both with heavy meromyosin and with subfragment-1. Considering the accuracy and the number of accessible residues in proteins, it is estimated that 4 tyrosyl and 1 tryptophanyl residues are buried into the interior of the protein molecule per one site of ES-complex accompanying the UV spectral change." @default.
- W2129675399 created "2016-06-24" @default.
- W2129675399 date "1971-01-01" @default.
- W2129675399 modified "2023-10-17" @default.
- W2129675399 title "Interaction of Heavy Meromyosin with Substrate<subtitle>IV. Studies on the Tyrosine and Tryptophan Residues by Solvent Perturbation Method<xref ref-type=fn rid=fn1><sup>*</sup></xref></subtitle>" @default.
- W2129675399 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a129488" @default.
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