Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …

Proteins exhibit structural fluctuations over decades of time scales. From the picosecond
side chain motions to aggregates that form over the course of minutes, characterizing protein …

Many of life's most fascinating phenomena emerge from interactions among many elements—
many amino acids determine the structure of a single protein, many genes determine the …

Protein folding should be complex. Proteins organize themselves into specific three-
dimensional structures, through a myriad of conformational changes. The classical view of …

Protein folding in the cell relies on the orchestrated action of conserved families of molecular
chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding …

The ensemble folding of two 21-residue α-helical peptides has been studied using all-atom
simulations under several variants of the AMBER potential in explicit solvent using a global …

The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and
controls the stability of select proteins. Emerging data explain how Hsp90 achieves client …

A large fraction of cellular proteins are oligomeric. Protein oligomerization may often be an
advantageous feature from the perspective of protein evolution and has probably evolved by …

Protein folding in the cell requires ATP-driven chaperone machines such as the conserved
Hsp70 and Hsp90. It is enigmatic how these machines fold proteins. Here, we show that …

Classical studies show that for many proteins, the information required for specifying the
tertiary structure is contained in the amino acid sequence. Here, we attempt to define the …