The bacterial chaperonin GroEL and its cofactor GroES constitute the paradigmatic
molecular machine of protein folding. GroEL is a large double-ring cylinder with ATPase …

Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …

Computational biology and bioinformatics provide vast data gold-mines from protein
sequences, ideal for Language Models (LMs) taken from Natural Language Processing …

In eukaryotic cells a molecular chaperone network associates with translating ribosomes,
assisting the maturation of emerging nascent polypeptides. Hsp70 is perhaps the major …

Cells face a constant challenge as they produce new proteins. The newly synthesized
polypeptides must be folded properly to avoid aggregation. If proteins do misfold, they must …

Limited understanding of human proteoforms with complex posttranslational modifications
and the underlying mechanisms poses a major obstacle to research on human health and …

The routine transformation of a liquid, as it is rapidly cooled, resulting in glass formation, is
remarkably complex. A theoretical explanation of the dynamics associated with this process …

The GroEL/ES chaperonin system functions as a protein folding cage. Many obligate
substrates of GroEL share the (βα) 8 TIM-barrel fold, but how the chaperonin promotes …

We demonstrate a generalizable strategy to use the relative trajectories of pairs and groups
of nanocrystals, and potentially other nanoscale objects, moving in solution which can now …

All processes that occur within living organisms are intimately linked to biological
macromolecules such as proteins, nucleic acids, or polysaccharides. Phospholipid …