Amyloid-like Fibrils from an α-Helical Transmembrane Protein.

ABSTRACT: The propensity to misfold and self-assemble into stable aggregates is increasingly being recognized as a common feature of protein molecules. Our understanding of this phenomenon and of its links with human disease has improved substantially over the past two decades. Studies thus far, however, have been almost exclusively focused on cytosolic proteins, resulting in a lack of detailed information about the misfolding and aggregation of membrane proteins. As a consequence, although such proteins make up approximately 30% of the human proteome and have high propensities to aggregate, relatively little is known about the biophysical nature of their assemblies. To shed light on this issue, we have studied as a model system an archetypical representative of the ubiquitous major facilitator supe

SUBMITTER: Stroobants K 

PROVIDER: S-EPMC5489960 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature