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Updated: Jul 17, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
[Study of protein conformation in solution by tyrosine residues RRS spectrum]
Yuan Zhang1, Zhe-xuan Lin, Hui Li
1Central Laboratory, Shantou University Medical College, Shantou 515041, China.
Abstract:
Due to the interference caused by the emission of tryptophan residue, it is hard to use fluorospectrophotometry to detect the spectrometric changes of the tyrosine residue when protein conformation is changed. When the concentration of protein in solution is relatively high, tyrosine residue has a characteristic scattering peak when excited with its K-band wavelength of light. In the present study, the authors established a method for detecting protein conformation changes in solution through the changes (peak height and wavelength shift) of the characteristic scattering peak of tyrosine residue. The method may be used for detecting protein conformation changes in solution caused by the changes of electrolyte, pH, and temperature.
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