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 …

Protein degradation is a necessity for many reasons: Homeostasis must be maintained while
cellular structures are continually rebuilt, in particular during development or in response to …

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 …

The atomic force microscope (AFM) has a unique capability of allowing the high-resolution
imaging of biological samples on substratum surfaces in physiological solutions. Recent …

High-speed atomic force microscopy (HS-AFM) is now materialized. It allows direct
visualization of dynamic structural changes and dynamic processes of functioning biological …

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 …

Proteins are linear polymers synthesized by ribosomes from activated amino acids. The
product of this biosynthetic process is a polypeptide chain, which has to adopt the unique …

Recent structural and biochemical investigations have come together to allow a better
understanding of the mechanism of chaperonin (GroEL, Hsp60)–mediated protein folding …

CHAPERONINS are ring-shaped protein complexes that are essential in the cell, mediating
ATP-dependent polypeptide folding in a vari-ety of compartments1–3. Recent studies …

We have determined to 2.6 Å resolution the crystal structure of the thermosome, the archaeal
group II chaperonin from T. acidophilum. The hexadecameric homolog of the eukaryotic …