Protein can release trapped histones in the cell

In the cell nucleus, histones play a crucial role packaging DNA into chromatin. Histones are however very sticky to both DNA and RNA, so to ensure they are transported to the cell nucleus after synthesis and bind to the right ...

Bringing bad proteins back into the fold

A study led by UT Southwestern has identified a mechanism that controls the activity of proteins known as chaperones, which guide proteins to fold into the right shapes. The findings, published online today in Nature Communications, ...

Unraveling one of prion disease's deadly secrets

A molecular biologist at the University of Massachusetts Amherst who has for decades studied the nightmarish group of fatal diseases caused by prions—chronic wasting disease in deer, mad cow in cattle and its human analog—credits ...

Study reveals dynamics of crucial immune system proteins

Of the many marvels of the human immune system, the processing of antigens by the class I proteins of the major histocompatability complex (MHC-I) is among the most mind-boggling. Exactly how these proteins carry out their ...

Study demonstrates 'tunability' of a molecular chaperone

For decades, molecular biologists studying a class of molecular chaperones known as heat shock proteins (Hsp70s) have relied on the Hsp70s found in bacteria as the model system. Now one of the world's experts on the molecule ...

Chaperones can hold protein in non-equilibrium states

Chaperones are specialized proteins in the cell that help other proteins to reach their functional 3-D shapes, which correspond to the states preferred at thermodynamic equilibrium. But a new study by EPFL, UNIL and INSERM ...

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