Modification of a specific tyrosine enables tracing of the end‐to‐end distance during apomyoglobin folding
- 23 October 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 374 (1) , 105-109
- https://doi.org/10.1016/0014-5793(95)01087-u
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.Keywords
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