In just three years, the green fluorescent protein (GFP) from the jellyfish Aequorea victoria
has vaulted from obscurity to become one of the most widely studied and exploited proteins …

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

The folding of many newly synthesized proteins in the cell depends on a set of conserved
proteins known as molecular chaperones. These prevent the formation of misfolded protein …

An essential cellular machinery that has been identified and studied only relatively recently
is a collective of specialized proteins, molecular chaperones, that bind nonnative states of …

▪ Abstract Recent years have witnessed dramatic advances in our understanding of how
newly translated proteins fold in the cell and the contribution of molecular chaperones to this …

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 …

Although phenomenlogical models that account for cooperativity in allosteric systems date
back to the early and mid‐60's (eg, the KNF and MWC models), there is resurgent interest in …

Kinesin motors power many motile processes by converting ATP energy into unidirectional
motion along microtubules. The force-generating and enzymatic properties of conventional …

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 …

The green fluorescent protein (GFP) from the jellyfish Aequorea victoria forms an intrinsic
chromophore through cyclization and oxidation of an internal tripeptide motif [Prasher, DC …