This review outlines the effect of disease-causing mutations on proteins' thermodynamics.
Two major thermodynamics quantities, which are essential for structural integrity, the folding …

Structural information of biological macromolecules is crucial and necessary to deliver
predictions about the effects of mutations—whether polymorphic or deleterious (ie, disease …

The development of methods and algorithms to predict the effect of mutations on protein
stability, protein–protein interaction, and protein–DNA/RNA binding is necessitated by the …

The first release of the Thermodynamic Database for Proteins and Mutants (ProTherm)
contains more than 3300 data of several thermodynamic parameters for wild type and …

It is of great interest from both scientific and practical viewpoints to theoretically predict the
thermal-stability changes upon mutations of a protein. However, such a prediction is an …

In vitro thermal denaturation experiments suggest that, because of the possibility of
irreversible alterations, thermodynamic stability (ie, a positive value for the unfolding Gibbs …

Recently, a number of methods have been proposed that are designed to extract
contributions to the change in free energy associated with a given perturbation or mutation …

The coupling of protein energetics and sequence changes is a critical aspect of
computational protein design, as well as for the understanding of protein evolution, human …

Protein side-chain mutation is fundamental both to natural evolutionary processes and to the
engineering of protein therapeutics, which constitute an increasing fraction of important …

Revealing the molecular effect that pathogenic missense mutations have on the
corresponding protein is crucial for developing therapeutic solutions. This is especially …