Upon biological self-assembly, the number of accessible translational configurations of
water in the system increases considerably, leading to a large gain in water entropy. It is …

We briefly review our studies on the folding/unfolding mechanisms of proteins. In biological
self-assembly processes such as protein folding, the number of accessible translational …

It is a central issue to elucidate the new type of molecular recognition accompanied by a
global structural change of a molecule upon binding to its targets. Here we investigate the …

Proteins are unique natural macromolecules with high selectivity and efficiency for their
functions. Understanding the chemical reaction mechanisms of proteins has long been an …

The configurational entropy of solute molecules is a crucially important quantity to study
various biophysical processes. Consequently, it is necessary to establish an efficient …

Privalov and co-workers estimated the changes in hydration enthalpy and entropy upon
ubiquitin unfolding and their temperature dependences denoted by Δ H hyd (T) and Δ S hyd …

In earlier works, we showed that the entropic effect originating from the translational
displacement of water molecules plays the pivotal role in protein folding and denaturation …

It is experimentally known that the heat-denaturation temperature of a protein is raised by
sugar addition [1]. In earlier work [2], we proposed a measure of the thermal stability of a …

In water, poly (N-isopropylacrylamide)(PNIPAM) is in a soluble coil state below the lower
critical soluble temperature (LCST) but in an insoluble globule state above LCST. Namely …

We investigate the effects of solvent specificities on the stability of the native structure (NS) of
a protein on the basis of our free-energy function (FEF). We use CPB-bromodomain (CBP …