Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Biologically active proteins are useful for studying the biological functions of genes and for
the development of therapeutic drugs and biomaterials in a biotechnology industry …

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

Cytochrome c (cyt c) is a cationic hemoprotein of∼ 100 amino acid residues that exhibits
exceptional functional versatility. While its primary function is electron transfer in the …

In this study, we had exploited the advancement in computer technology to determine the
stability of four apomyoglobin variants namely wild type, E109A, E109G and G65A/G73A by …

We employ molecular dynamics simulations to study the solubility and molecular
conformations of n-alkane chains in water. We find nearly exponential decrease in solubility …

The hydrophobic interaction drives nonpolar solutes to aggregate in aqueous solution, and
hence plays a critical role in many fundamental processes in nature. An important property …

Protein folding research stalled for decades because conventional experiments indicated
that proteins fold slowly and in single strokes, whereas theory predicted a complex interplay …

Protein biosynthesis is inherently coupled to cotranslational protein folding. Folding of the
nascent chain already occurs during synthesis and is mediated by spatial constraints …

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 …