Proteins are dynamic entities that undergo a plethora of conformational changes that may
take place on a wide range of time scales. These changes can be as small as the rotation of …

Psychrophiles thriving permanently at near‐zero temperatures synthesize cold‐active
enzymes to sustain their cell cycle. Genome sequences, proteomic, and transcriptomic …

Orthologous proteins of species adapted to different temperatures exhibit differences in
stability and function that are interpreted to reflect adaptive variation in structural “flexibility.” …

Cold-adapted enzymes from psychrophilic species show the general characteristics of being
more heat labile, and having a different balance between enthalpic and entropic …

Comparative studies of orthologous proteins of species evolved at different temperatures
have revealed consistent patterns of temperature-related variation in thermal stabilities of …

Commercial food and l-amino acid industries rely on bioengineered d-amino acid oxidizing
enzymes to detect and remove d-amino acid contaminants. However, the bioengineering of …

Cold-adapted enzymes exhibit enhanced conformational flexibility, especially in their active
sites, as compared with their warmer-temperature counterparts. However, the mechanism by …

Conformational flexibility of proteins provides enzymes with high catalytic activity. Although
the conformational flexibility is known to be pivotal for the ligand binding and release, its role …

The investigation of the structural determinants of enzymatic temperature adaptation is a
crucial pre-requisite both in terms of fundamental research and industrial applications to …

The physicochemical bases for enzyme cold-adaptation remain elusive. The current view is
that psychrophilic enzymes are often characterized by enhanced flexibility at low …