For the last few years, molten salt nanomaterials have attracted many scientists for their enhanced specific heat by doping a minute concentration of nanoparticles (up to 1% by weight). Likewise, enhancing the specific heat of liquid media is important in many aspects of engineering such as engine oil, coolant, and lubricant. However, such enhancement in specific heat was only observed for molt...

The molten globular conformation of V26A ubiquitin (valine to alanine mutation at residue 26) was studied by nuclear magnetic resonance spectroscopy in conjunction with amide hydrogen/deuterium exchange. Most of the amide protons that are involved in the native secondary structures were observed to be protected in the molten globule state with the protection factors from 1.2 to 6.7. These prote...

The structure of molten LaBr3 was investigated by X-ray diffraction and molecular dynamics simulations. It was found that the short range structure of molten LaBr3 is very similar to that of molten LaCl3, except for some structural features such as interionic distances based on the difference of anion sizes. In the MD simulation, the shear viscosity of molten LaBr3 was estimated from the struct...

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for the study of the structure, dynamics, and folding of proteins in solution. It is particularly powerful when applied to dynamic or flexible systems, such as partially folded molten globule states of proteins, which are not usually amenable to X-ray crystallography. In this article, NMR methods suitable for the detailed cha...

Polyethylene glycol has been shown to bind to the molten globule intermediate on the bovine carbonic anhydrase B folding pathway. The mechanism of this interaction has been extensively probed. Polyethylene glycol (PEG) binds weakly to the molten globule first intermediate as measured by hydrophobic interaction chromatography, but PEG does not bind to either the native state or the second interm...