The chaperonins are ubiquitous and essential nanomachines that assist in protein folding in
an ATP-driven manner. They consist of two back-to-back stacked oligomeric rings with …

Due to advances in methods for site-specific incorporation of unnatural amino acids (UAAs)
into proteins, a large number of UAAs with tailored chemical and/or physical properties have …

Variable-temperature electrospray ionization (vT-ESI) native mass spectrometry (nMS) is
used to determine the thermodynamics for stepwise binding of up to 14 ATP molecules to …

Confining compartments are ubiquitous in biology, but there have been few experimental
studies on the thermodynamics of protein folding in such environments. Recently, we …

Fluorescence correlation spectroscopy and time-dependent fluorescence Stokes shift have
been employed to elucidate dynamics in different time scales, ranging from picoseconds to …

Hypothesis Lamellar gels are widely formulated in household and cosmetic products
because of their eminent ability to improve long-term stability of thermodynamically unstable …

Spatial confinement significantly affects protein folding. Without the confinement provided by
chaperones, many proteins cannot fold correctly. However, the quantitative effect of …

Protein-protein interactions are at the basis of many protein functions, and the knowledge of
3D structures of protein-protein complexes provides structural, mechanical and dynamical …

The structure of the carbon nanotube affects water transport greatly. However, there is little
understanding of water transport through the inward combined carbon nanotube. Molecular …

Cellular functions are governed by a myriad of processes that typically occur through
multiple steps, spanning an astonishingly wide time-window from femtoseconds to seconds …