Unfolding thermodynamics of cysteine-rich proteins and molecular thermal-adaptation of marine ciliates.

ABSTRACT: Euplotes nobilii and Euplotes raikovi are phylogenetically closely allied species of marine ciliates, living in polar and temperate waters, respectively. Their evolutional relation and the sharply different temperatures of their natural environments make them ideal organisms to investigate thermal-adaptation. We perform a comparative study of the thermal unfolding of disulfide-rich protein pheromones produced by these ciliates. Recent circular dichroism (CD) measurements have shown that the two psychrophilic (E. nobilii) and mesophilic (E. raikovi) protein families are characterized by very different melting temperatures, despite their close structural homology. The enhanced thermal stability of the E. raikovi pheromones is realized notwithstanding the fact that these proteins form, as a r

SUBMITTER: Cazzolli G 

PROVIDER: S-EPMC4030967 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature