| Title: | Thermodynamic stability of psychrophilic and mesophilic pheromones of the protozoan ciliate euplotes |
| Author(s): | Geralt M; Alimenti C; Vallesi A; Luporini P; Wuthrich K; |
| Address: | "Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. mgeralt@scripps.edu. Department of Environmental and Natural Sciences, University of Camerino, Camerino 62032, Italy. claudio.alimenti@unicam.it. Department of Environmental and Natural Sciences, University of Camerino, Camerino 62032, Italy. adriana.vallesi@unicam.it. Department of Environmental and Natural Sciences, University of Camerino, Camerino 62032, Italy. piero.luporini@unicam.it. Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. wuthrich@mol.biol.ethz.ch" |
| ISSN/ISBN: | 2079-7737 (Print) 2079-7737 (Electronic) 2079-7737 (Linking) |
| Abstract: | "Three psychrophilic protein pheromones (En-1, En-2 and En-6) from the polar ciliate, Euplotes nobilii, and six mesophilic pheromones (Er-1, Er-2, Er-10, Er-11, Er-22 and Er-23) from the temperate-water sister species, Euplotes raikovi, were studied in aqueous solution for their thermal unfolding and refolding based on the temperature dependence of their circular dichroism (CD) spectra. The three psychrophilic proteins showed thermal unfolding with mid points in the temperature range 55-70 degrees C. In contrast, no unfolding was observed for any of the six mesophilic proteins and their regular secondary structures were maintained up to 95 degrees C. Possible causes of these differences are discussed based on comparisons of the NMR structures of the nine proteins" |
| Notes: | "PubMed-not-MEDLINEGeralt, Michael Alimenti, Claudio Vallesi, Adriana Luporini, Pierangelo Wuthrich, Kurt eng Switzerland 2013/01/01 Biology (Basel). 2013 Jan 14; 2(1):142-50. doi: 10.3390/biology2010142" |
