Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins

Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins

Sequences rich in glutamine (Q) and asparagine (N) residues often fail to fold at the monomer level. This, coupled to their unusual hydrogen-bonding abilities, provides the driving force to switch between disordered monomers and amyloids. Such transitions govern processes as diverse as human protein...

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Main Authors: Halfmann, Randal Arthur (Contributor), Alberti, Simon (Author), Krishnan, Rajaraman (Author), Lyle, Nicholas (Author), O'Donnell, Charles William (Contributor), King, Oliver D. (Author), Berger, Bonnie (Contributor), Pappu, Rohit V (Author), Lindquist, Susan (Contributor)
Other Authors: Massachusetts Institute of Technology. Computer Science and Artificial Intelligence Laboratory (Contributor), Massachusetts Institute of Technology. Department of Biology (Contributor), Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science (Contributor), Massachusetts Institute of Technology. Department of Mathematics (Contributor), Whitehead Institute for Biomedical Research (Contributor)
Format: Article
Language:English
Published: Elsevier, 2014-12-16T14:29:21Z.
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