Efficient folding of many newly synthesized proteins depends on assistance from molecular
chaperones, which serve to prevent protein misfolding and aggregation in the crowded …

Complex processes are involved in the protection of cells and organisms by heat shock
proteins (hsps). Aberrant protein production due to high temperatures is prevented by the …

The term “Glomalin” was originally used to describe a hypothetical gene product of
arbuscular mycorrhizal fungi (AMF) that was assumed to be a nearly ubiquitous …

In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid
sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the …

Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit
protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli …

The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made
of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry …

There is a growing concern about the increase in human morbidity and mortality caused by
foodborne pathogens. Antibiotics were and still are used as the first line of defense against …

Protein folding in vivo is mediated by an array of proteins that act either as 'foldases' or
'molecular chaperones'. Foldases include protein disulfide isomerase and peptidyl prolyl …

The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by
sequestering nonnative polypeptides in a cage-like structure. Here we define the …

Bacilli secrete numerous proteins into the environment. Many of the secretory proteins, their
export signals, and their processing steps during secretion have been characterized in …