Increasing the temperature by just a few degrees may lead to structural perturbation or
unfolding of the protein and consequent loss of function. The concepts of flexibility and …

The molecular bases of thermal and cold stability and adaptation, which allow proteins to
remain folded and functional in the temperature ranges in which their host organisms live …

Optimum protein function and biochemical activity critically depends on water availability
because solvent thermodynamics drive protein folding and macromolecular interactions …

ProThermDB is an updated version of the thermodynamic database for proteins and mutants
(ProTherm), which has∼ 31 500 data on protein stability, an increase of 84% from the …

The liquid–liquid phase separation (LLPS) of intrinsically disordered proteins (IDPs) is a
commonly observed phenomenon within the cell, and such condensates are also highly …

Natural enzymes are delicate biomolecules possessing only marginal thermodynamic
stability. Poorly stable, misfolded, and aggregated proteins lead to huge economic losses in …

Thermostable proteins find their use in numerous biomedical and biotechnological
applications. However, the computational design of stable proteins often results in single …

There is a continuous interest in increasing proteins stability to enhance their usability in
numerous biomedical and biotechnological applications. A number of in silico tools for the …

Enzyme immobilization is an essential technology for commercializing biocatalysis. It
imparts stability, recoverability, and other valuable features that improve the effectiveness of …

The use of enzymes for industrial and biomedical applications is limited to their function at
elevated temperatures. The principles of thermostability engineering need to be …