Proceedings of the Eighth Conference on Time-Resolved Vibrational SpectroscopyView this Special Issue
H. Georg, C. W. Wharton, F. Siebert, "Temperature Induced Protein Unfolding and Folding of RNase a Studied by Time-Resolved Infrared Spectroscopy", Laser Chemistry, vol. 19, Article ID 028202, 3 pages, 1999. https://doi.org/10.1155/1999/28202
Temperature Induced Protein Unfolding and Folding of RNase a Studied by Time-Resolved Infrared Spectroscopy
When a protein finds its native three-dimensional structure from the unstructured amino-acid chain various processes spanning a large time range are relevant. To understand the mechanism of protein folding one needs to cover the entire folding/ refolding (U↔N) reaction on a structural level. In the case of RNase A, the main structural changes occur in the ms time range, that can be monitored with rapid-scan- FTIR spectroscopy combined with rapid mixing techniques. To induce unfolding we inject aqueous protein solution into a hot IR cuvette and record the time course of the spectral changes. A lag phase is found when the unfolding conditions are relatively weak, suggesting an unfolding intermediate.
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