Natural metalloenzymes with astonishing reaction activity and specificity underpin essential
life transformations. Nevertheless, enzymes only operate under mild conditions to keep …

All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

Substantial improvements in enzyme activity demand multiple mutations at spatially
proximal positions in the active site. Such mutations, however, often exhibit unpredictable …

Enzymes must be ordered to allow the stabilization of transition states by their active sites,
yet dynamic enough to adopt alternative conformations suited to other steps in their catalytic …

The growing interest for comparing protein internal dynamics owes much to the realisation
that protein function can be accompanied or assisted by structural fluctuations and …

Enzymes found in nature have been exploited in industry due to their inherent catalytic
properties in complex chemical processes under mild experimental and environmental …

Enzymes are dynamic entities, and their dynamic properties are clearly linked to their
biological function. It follows that dynamics ought to play an essential role in enzyme …

Organismal adaptation to extreme temperatures yields enzymes with distinct configurational
stabilities, including thermophilic and psychrophilic enzymes, which are adapted to high and …

Optimization processes, such as evolution, are constrained by diminishing returns—the
closer the optimum, the smaller the benefit per mutation, and by tradeoffs—improvement of …

Multidimensional fitness landscapes provide insights into the molecular basis of laboratory
and natural evolution. To date, such efforts usually focus on limited protein families and a …