Hydrophilized graphene prevents protein denaturation at the air-water interface.

The β-barrel conformation of the KOW domain of the metamorphic protein RfaH is in equilibrium with a low-populated, predominately unstructured state exhibiting helical elements, suggesting that transiently structured elements in unfolded conformations might be a general scheme in fold-switching proteins.

C-mannosylation supports native folding of thrombospondin type 1 repeats in the endoplasmic reticulum and stabilizes the folded proteins by modulating the dynamics of the tryptophan-arginine ladder.

Fiducial-less tomography on single particle cryoEM samples reveals that most particles are adsorbed to the air-water interface and allows for researchers to diagnose and solve sample, grid, ice thickness, collection, and processing issues.

Both the polypeptide and attached O-glycans N-terminal to the A1 domain in von Willebrand factor lower its affinity for its ligand GPIbα on platelets, its stability, and structural dynamics and decrease population of a high-affinity, intermediate state in unfolding.

Fixed, intact animals of C. elegans can be physically expanded with high isotropy, to enable super-resolved imaging of general proteins and nucleic acids throughout the organism, on conventional microscopes.

The small molecule EMD 57033 is one of a new class of pharmacological chaperones that stabilize, enhance the activity of, and correct stress-induced misfolding of myosin proteins.

A fully synthetic library of humanized single domain antibodies yields in vitro high affinity antibodies usable in cell biology and translational projects.

Recovery of proteins from aggregates by Hsp70 is boosted by the Hsp110 co-chaperone, which promotes abundant Hsp70 recruitment to aggregates and supports initial aggregate remodelling into small assemblies.

A fast evolutionary approach to engineer membrane protein kinetic stability yields folded excitatory neurotransmitter transporters and provides insights into their denaturing pathway.