Chaperones support protein folding in different cellular compartments and some chaperones associate with ribosomes to help fold newly synthesized proteins. Two studies by Koplin et al. and Albanèse et ...

The first full-length structures of two heat shock chaperone proteins in a complex reveal the key structural region regulating their function, according to a new study from St. Jude Children's ...

Intrinsically disordered proteins (IDPs) lack well-defined structure but are widely represented in eukaryotic proteomes. Although the functions of most IDPs are not understood, some have been shown to ...

Like a parent of teenagers at a party, Mother Nature depends on chaperones to keep one of her charges, the immune system, in line so that it doesn't mistakenly attack normal cells, tissues and organs ...

In a new study, researchers are learning more about how ribosome chaperones work, showing that one particular chaperone binds to its protein client in a very specific, tight manner, almost like a ...

A recent study from CU Boulder researchers shows that cells must actively work to keep sticky molecules, known as ribonucleic acid (RNA), apart, or they may form large assemblies that could cause ...

The Hsp70 class of heat shock proteins (Hsps) has been implicated at multiple points in the immune response, including initiation of proinflammatory cytokine production, antigen recognition and ...

In order to fulfil their many functions, proteins must be folded into the correct shape. Researchers at the University of Basel have now discovered tiny “folding factories” in cells that enable ...

MANHATTAN, Kansas -- A Kansas State University-led study is helping uncover the intricate workings of how a specific "molecular machine" inside of cells is assembled. Fully understanding this process ...

Two chaperone proteins in humans -- DO and DM -- work together to assist the presentation of antigens so that the immune system correctly determines that they are foreign and not normal, healthy ...