Thermodynamics Research Today is a free monthly online journal that collates and summarizes the latest research about Thermodynamics, including details on enthalpy, entropy, energy transitions. | ||||||||
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Secreted glycoprotein from Live Zaire ebolavirus-infected cultures: preparation, structural and biophysical characterization, and thermodynamic stability.Barrientos LG, Martin AM, Wohlhueter RM, Rollin PE Special Pathogens Branch, Division of Viral and Rickettsial Diseases, National Center for Zoonotic, Vector-Borne, and Enteric Diseases, Centers for Disease Control and Prevention, Atlanta, GA 30333, USA. LBarrientos1@cdc.gov Milligram quantities of Zaire ebolavirus nonstructural, secreted glycoprotein (sGP) were purified to homogeneity, and this preparation was characterized by an array of biophysical and biochemical experiments. Mass-spectrometry analysis revealed sGP posttranslational modifications and regions susceptible to limited proteolysis. In solution, sGP has an absolute molar mass of 103 kDa, is monodisperse, and folds into a predominantly beta -sheet conformation with a distinct tertiary structure. sGP appears to have a unique free-energy landscape that facilitates reversible folding and a strong propensity for disulfide-linked dimeric quaternary structure under a wide range of conditions; the low apparent free energy of conformation transition of sGP ( Delta G=1.7+/-0.1 kcal/mol) suggests that the molecule is well suited as a thermodynamically facile switch, which would allow it to report on relatively subtle changes in milieu. In addition, a conformational transition at 37 degrees C was detected in thermal denaturing experiments. On the basis of biophysical and biochemical considerations alone, we propose that the property of being a thermodynamically facile switch is an important clue to reveal sGP functionality. Published 17 October 2007 in J Infect Dis, 196: S220-31.
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