Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2053266 | FEBS Letters | 2005 | 6 Pages |
Abstract
The lack of a membrane environment in membrane protein crystals is considered one of the major limiting factors to fully imply X-ray structural data to explain functional properties of ion channels [Gulbis, J.M. and Doyle, D. (2004) Curr. Opin. Struct. Biol. 14, 440–446]. Here, we provide infrared spectroscopic evidence that the structure and stability of the potassium channel KcsA and its chymotryptic derivative 1–125 KcsA reconstituted into native-like membranes differ from those exhibited by these proteins in detergent solution, the latter taken as an approximation of the mixed detergent-protein crystal conditions.
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Authors
J.A. Encinar, M.L. Molina, J.A. Poveda, F.N. Barrera, M.L. Renart, A.M. Fernández, J.M. González-Ros,