Subcellular processes, from molecular events to organellar responses and cell movement,
cover a broad scale in time and space. Clearly the extremes, such as ion channel activation …

This article describes the molecular mechanism by which tetraalkylammonium chloride ([R 4
N] Cl: R-= methyl (Me), ethyl (Et), propyl (Pr), butyl (Bu)) modulates the stability, folding, and …

The infrared (IR) absorption of the amide I band for the loop structure may overlap with that
of the α-helices, which can lead to the misassignment of the protein secondary structures. A …

Unfolded vs native CO-coordinated horse heart cytochrome c (h-cyt c) and a heme axial
methionine mutant cyt c 552 from Hydrogenobacter thermophilus (Ht-M61A) are studied by …

This paper analyzes the effect of pH on thermodynamic stability and folding kinetics of horse
cytochrome c (cyt c). Analysis of equilibrium unfolding transitions of Ferricyt c and Ferrocyt c …

This manuscript determines the factors by which the water-miscible ionic liquid (IL), 1-alkyl-3-
methylimidazolium chloride [Rmim] Cl affects the thermodynamic stability and CO …

It is well-known that hydrophobic effect play a major role in alcohol–protein interactions
leading to structure unfolding. Studies with extremely alkaline cytochrome c (UB state, pH …

This paper describes the structural and dynamic properties of a hitherto uncovered alkali
molten globule (MG) state of horse “ferrocytochrome c”(ferrocyt c). Several experimental …

An orderly investigation of the levels of secondary and tertiary structures, kinetics of tertiary
structural changes, and self diffusion coefficient of lysozyme and cytochrome c in the …

The folding of reduced cytochrome c (redcyt c) is increasingly being recognized as
undergoing a mechanism that deviates from a two-state process. In previous far-UV TRORD …