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- W1546548688 abstract "Abstract Optical rotation measurements and absorption difference spectroscopy of ribonuclease A in different water-acetic acid mixtures showed that at least three conformational situations exist for the protein molecule at different levels of acetic acid concentration. Hematoporphyrin-sensitized photooxidation of the native as well as of the denatured proteins allowed us to detect three discrete states of reactivity for the 4 methionyl residues of ribonuclease A. On the basis of the photooxidation kinetics and of the conformational analyses, we concluded that methionine-29 is partly exposed in the native protein and methionine-13 is partially buried, whereas methionine-30 and methionine-79 are deeply buried. The importance of the single methionyl residues for the catalytic activity of the enzyme has been also resolved. The described procedure appears to be a reliable tool for examining the state of the amino acid residues in proteins." @default.
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- W1546548688 date "1970-07-01" @default.
- W1546548688 modified "2023-10-07" @default.
- W1546548688 title "Dye-sensitized Photooxidation As a Tool for Determining the Degree of Exposure of Amino Acid Residues in Proteins" @default.
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- W1546548688 doi "https://doi.org/10.1016/s0021-9258(18)63006-6" @default.
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