The goal of this article is to summarize what has been learned about the major forces
stabilizing proteins since the late 1980s when site-directed mutagenesis became possible …

A number of machine learning (ML)-based algorithms have been proposed for predicting
mutation-induced stability changes in proteins. In this critical review, we used hypothetical …

The denatured state ensemble (DSE) of unfolded proteins, once considered to be well-
modeled by an energetically featureless random coil, is now well-known to contain flickering …

In this work, to unveil the substituent effect on the excited-state intramolecular proton transfer
(ESIPT) reaction of 1, 8-Dihydroxyanthraquinone (DHAQ), four derivatives DHAQ-Me, DHAQ …

Polypeptide chain collapse is an integral component of a protein folding reaction. In this
review, experimental characterization of the interplay of polypeptide chain collapse …

This study aims to determine the antibacterial efficacy of a bioactive phytochemical quercetin
(QUR), compared to the reference antibiotic ciprofloxacin (CIP), using in vitro and in silico …

Experimental measurements and computational results have shown that polypeptide chains,
made up of 15–25 glycine residues, collapse to compact structures in water at room …

Non‐equilibrium molecular dynamics simulations of a solvated 21‐residue polyalanine
(A21) peptide, featuring a high propensity for helix formation, have been performed at 300 K …

Protein structures are stabilized by a variety of noncovalent interactions (NCIs), including the
hydrophobic effect, hydrogen bonds, electrostatic forces and van der Waals' interactions …

Protein folding evolves by exploring the conformational space with a subtle balance
between enthalpy and entropy changes which eventually leads to a decrease of free energy …