A glass menagerie of low complexity sequences.
Remarkably simple proteins play outsize roles in the execution of developmental complexity within biological systems. Sequence information determines structure and hence function, so how do low complexity sequences fulfill their functions? Recent discoveries are raising the curtain on a new dimension of the sequence-structure paradigm. In it, function derives not from the structures of individual proteins, but instead, from dynamic material properties of entire ensembles of the proteins acting in unison through phase changes. These phases include liquids, one-dimensional crystals, and - as elaborated herein - even glasses. The peculiar thermodynamics of glass-like protein assemblies, in particular, illuminate new principles of information flow through and, at times, orthogonal to the central dogma of molecular biology.
Stowers Institute for Medical Research, 1000 E. 50th St., Kansas City, MO 64110, USA; Department of Molecular and Integrative Physiology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA. Electronic address: rhn@stowers.org.
Randal
R
Halfmann
D000595:Amino Acid Sequence; D000818:Animals; D005898:Glass / Q000737:chemistry*; D006801:Humans; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D059748:Proteolysis; D013816:Thermodynamics
D011506:Proteins