Characterization of the rough endoplasmic reticulum ribosome-binding activity.

The rough endoplasmic reticulum membranes of mammalian cells contain specific ribosome-binding sites. A purification to apparent homogeneity of a negatively charged protein (ERp180) of relative molecular mass 180,000 (180 K) was reported which was proposed to function as a rough endoplasmic reticulum ribosome receptor. We report here that ribosome-binding site activity quantitatively solubilized from rough endoplasmic reticulum membranes does not cofractionate with ERp180. By contrast, ribosome-binding site activity fractionates as a much smaller, positively charged protein.     

Cartesian causation: body–body interaction, motion, and eternal truths

There is considerable debate among scholars over whether Descartes allowed for genuine body–body interaction. I begin by considering Michael Della Rocca’s recent claim that Descartes accepted such interaction, and that his doctrine of the creation of the eternal truths indicates how this interaction could be acceptable to him. Though I agree that Descartes was inclined to accept real bodily causes of motion, I differ from Della Rocca in emphasizing that his ontology ultimately does not allow for them. This is not the end of the story however, since two of Descartes’s successors offered incompatible ways of developing his conflicted account of motion. I contrast the occasionalist view of Nicolas Malebranche that changes in motion derive directly from divine volitions with the non-occasionalist claim of Pierre-Sylvain Regis that such changes derive from a nature distinct from God. In light of Della Rocca’s interpretation, it is noteworthy that the issue of eternal truths is relevant to both alternative accounts. Indeed, Regis took the doctrine that such truths are created to provide crucial support for his alternative to an occasionalist account of body–body interaction. What does not help Della Rocca, however, is that Regis’s view of motion requires a fundamental revision of Descartes’s ontology.     

Structural Changes of Water Molecules Upon the Reduction of Quinones in The Reaction Center from Rhodobactery Sphaeroides

1 Results The photosynthetic bacterial reaction center (RC) is a membrane protein complex.The RC is composed of three protein subunits and redox components such as bacteriochlorophylls, bacteriopheophytins,and quinones.The RC performs the photochemical electron transfer from the bacteriochlorophyll dimer through a series of electron donor and acceptor molecules to a secondary quinone,QB.QB accepts electrons from a primary quinone,QA,in two sequential electron transfer reactions.The second electron trans...