Abstract
Changes in the secondary structure of cytochrome c on immersion in methanol were monitored using circular dichroism. These changes occurred immediately in methanol, upon re-immersion in aqueous buffer, the secondary structure was restored in ca. 45 min. This method enables the secondary structure of proteins in non-aqueous solvents to be monitored in real time.
Original language | English |
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Pages (from-to) | 10093-10097 |
Number of pages | 5 |
Journal | Physical Chemistry Chemical Physics |
Volume | 12 |
Issue number | 34 |
DOIs | |
Publication status | Published - 14 Sep 2010 |