The bacterial chaperonin GroEL and its cofactor GroES constitute the paradigmatic
molecular machine of protein folding. GroEL is a large double-ring cylinder with ATPase …

Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …

Molecular dynamics simulations and isothermal titration calorimetry (ITC) experiments with
neutral guests illustrate that the release of high-energy water from the cavity of cucurbit [n] …

Most proteins must fold into precise three-dimensional conformations to fulfill their biological
functions. Here we review recent concepts emerging from studies of protein folding in vitro …

Proteins generally must fold into precise three-dimensional conformations to fulfill their
biological functions. In the cell, this fundamental process is aided by molecular chaperones …

In recent years significant effort has been devoted to exploring the potential effects of
macromolecular crowding on protein folding and association phenomena. Theoretical …

The high concentration of macromolecules in the crowded cellular interior influences
different thermodynamic and kinetic properties of proteins, including their structural …

What are the molecular properties of proteins that fall on the radar of protein quality control
(PQC)? Here we mutate the E. coli's gene encoding dihydrofolate reductase (DHFR) and …

In this work, we combine atomistic molecular dynamics simulations with theoretical
vibrational spectroscopy to study the properties of water confined inside bis (2-ethylhexyl) …

Biological nanopores are a class of membrane proteins that open nanoscale water conduits
in biological membranes. When they are reconstituted in artificial membranes and a bias …