Maintaining the structure of protein and peptide drugs has become one of the most important
goals of scientists in recent decades. Cold and thermal denaturation conditions …

Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …

Abstract Cytochrome-c (cyt-c), a multi-functional protein, plays a significant role in the
electron transport chain, and thus is indispensable in the energy-production process …

A thermodynamically and kinetically simple picture of protein folding envisages only two
states, native (N) and unfolded (U), separated by a single activation free energy barrier, and …

Novel drug candidates are continuously being developed to combat the most life-
threatening diseases; however, many promising protein therapeutics are dropped from the …

Talin as a critical focal adhesion mechanosensor exhibits force-dependent folding dynamics
and concurrent interactions. Being a cytoplasmic protein, talin also might interact with …

Dry molten globular (DMG) intermediates, an expanded form of the native protein with a dry
core, have been observed during denaturant-induced unfolding of many proteins. These …

We propose a simple approach, based on the minimization of the total (entropic plus
unfolding) energy of a two-state system, to describe the unfolding of multi-domain …

The denaturation mechanism of hen egg lysozyme is still controversial. In this study, Raman
spectroscopy was employed to study the thermal and chemical denaturation mechanisms of …

Dissecting a protein unfolding process into individual steps can provide valuable information
on the forces that maintain the integrity of the folded structure. Solvation of the protein core …