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• W2000482037 abstract "In order to follow the overall geometry of the apomyoglobin molecule during folding, we have converted a specific tyrosine residue into 3‐nitro‐tyrosine. The specificity of the modification was verified by proteolytic cleavage of the modified protein and mass spectroscopy of the resulting fragments. By measuring the energy transfer from the tryptophanyl side‐chains to the modified residue the average end‐to‐end distance can be followed. The experiment shows that after initiation of folding the N‐ and C‐termini are rapidly brought into proximity, possibly to a near‐native distance." @default.
• W2000482037 created "2016-06-24" @default.
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• W2000482037 date "1995-10-23" @default.
• W2000482037 modified "2023-10-17" @default.
• W2000482037 title "Modification of a specific tyrosine enables tracing of the end-to-end distance during apomyoglobin folding" @default.
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• W2000482037 doi "https://doi.org/10.1016/0014-5793(95)01087-u" @default.
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