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Modification of a specific tyrosine enables tracing of the end‐to‐end distance during apomyoglobin folding
Author(s) -
Rischel Christian,
Poulsen Flemming M.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01087-u
Subject(s) - chemistry , tyrosine , folding (dsp implementation) , cleavage (geology) , biophysics , protein folding , crystallography , residue (chemistry) , stereochemistry , biochemistry , biology , paleontology , fracture (geology) , electrical engineering , engineering
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.