The area of biocatalysis itself is in rapid development, fueled by both an enhanced
repertoire of protein engineering tools and an increasing list of solved problems …

The strategy of rational design to engineer enzymes is to predict the potential mutants based
on the understanding of the relationships between protein structure and function, and …

The past several years have seen novel insights at the interface of protein biophysics and
evolution. The accepted paradigm that proteins can tolerate nearly any amino acid …

The limitations associated with natural enzyme catalysis have triggered the rise of the field of
protein engineering. Traditional rational design was based on the analysis of protein …

Natural proteins are often only slightly more stable in the native state than the denatured
state, and an increase in environmental temperature can easily shift the balance toward …

Commercial biocatalysis requires robust enzymes that can withstand elevated temperatures
and long incubations. Ancestral reconstruction has shown that pre-Cambrian enzymes were …

Engineering proteins for thermostability is an exciting and challenging field since it is critical
for broadening the industrial use of recombinant proteins. Thermostability of proteins arises …

A central goal in molecular evolution is to understand the ways in which genes and proteins
evolve in response to changing environments. In the absence of intact DNA from fossils …

SpyTag is a peptide that spontaneously forms an amide bond with its protein partner
SpyCatcher. SpyTag was fused at the N terminus of β‐lactamase and SpyCatcher at the C …

What changes occur when a natural protein that had been under low mutation rates is
subjected to a neutral drift at high mutational loads, thus generating genetically diverse …