“How do proteins fold?” Researchers have been studying different aspects of this question
for more than 50 years. The most conceptual aspect of the problem is how protein can find …

There are several important questions on the coupling between properties of the protein
shape and the rate of protein folding. We have studied a series of structural descriptors …

The number of protein and peptide structures included in Protein Data Bank (PDB) and Gen
Bank without functional annotation has increased. Consequently, there is a high demand for …

Inter-residue interactions in protein structures provide valuable insights into protein folding
and stability. Understanding these interactions can be helpful in many crucial applications …

Background The residue-wise contact order (RWCO) describes the sequence separations
between the residues of interest and its contacting residues in a protein sequence. It is a …

The time it takes for proteins to fold into their native states varies over several orders of
magnitude depending on their native‐state topology, size, and amino acid composition. In a …

The correlations between the logarithm of the unfolding rate of 108 proteins and their
structural parameters were calculated. We showed that there is a good correlation between …

Protein folding has been studied extensively for decades, yet our ability to predict how
proteins reach their native state from a mechanistic perspective is still rudimentary at best …

The sperm whale apomyoglobin pH 4 folding intermediate exists in two forms, Ia and Ib, that
mimic transient kinetic intermediates in the folding of the native protein at pH 6. To …

A major issue in molecular biology today is to understand how a protein folds into its
characteristic three-dimensional (3D) structure and how to gain its biological function as a …