Temperature Induced Protein Unfolding and Folding of RNase a Studied by Time-Resolved Infrared Spectroscopy

Autor:	H. Georg, F. Siebert, C. W. Wharton
Rok vydání:	1999
Předmět:	Cuvette Crystallography Aqueous solution Chemistry RNase P Phase (matter) Infrared spectroscopy Protein folding Folding (DSP implementation) Fourier transform infrared spectroscopy Biochemistry Spectroscopy Atomic and Molecular Physics and Optics
Zdroj:	Laser Chemistry. 19:233-235
ISSN:	1476-3516 0278-6273
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::f5fb7b8ac2f77847bc4327043e28b7ed https://doi.org/10.1155/1999/28202 Zobrazit plný text záznamu Plný text