Bacterial Inclusion Bodies Contain Amyloid-Like Structure

linked profile(s): Lei Wang
submitted by: apryl
Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, such as the hemoglobin molecules in sickle-cell fibrils, or can be reorganized β-sheet–rich aggregates, termed amyloid-like fibrils. Amyloid fibrils are associated with several...
Authors: David Eisenberg, Samir K Maji, Roland Riek, Michael R Sawaya, Lei Wang

Modern proteomes contain putative imprints of ancient shifts in trace metal geochemistry

submitted by: cdupont
Because of the rise in atmospheric oxygen 2.3 billion years ago (Gya) and the subsequent changes in oceanic redox state over the last 2.3–1 Gya, trace metal bioavailability in marine environments has changed dramatically. Although theorized to have influenced the biological usage of metals leaving discernable genomic signals, a thorough and quantitative test of this hypothesis has been lacking. Using structural bioinformatics and whole-genome sequences, the Fe-, Zn-, Mn-, and...
Authors: Christopher l. Dupont, Song Yang, Brian Palenik, Philip e. Bourne