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...
| Main Authors: | , , , , , , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
Elsevier
2014
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| Online Access: | http://hdl.handle.net/1721.1/92316 https://orcid.org/0000-0003-1307-882X https://orcid.org/0000-0002-2724-7228 |