Enzymes can be engineered at the level of their amino acid sequences to optimize key
properties such as expression, stability, substrate range, and catalytic efficiency─ or even to …

Directed evolution circumvents our profound ignorance of how a protein's sequence
encodes its function by using iterative rounds of random mutation and artificial selection to …

To reduce experimental effort associated with directed protein evolution and to explore the
sequence space encoded by mutating multiple positions simultaneously, we incorporate …

The amino acid sequence of a protein affects both its structure and its function. Thus, the
ability to modify the sequence, and hence the structure and activity, of individual proteins in …

Insertions and deletions (indels) enable evolution and cause disease. Due to technical
challenges, indels are left out of most mutational scans, limiting our understanding of them in …

The biophysical properties that enable proteins to so readily evolve to perform diverse
biochemical tasks are largely unknown. Here, we show that a protein's capacity to evolve is …

Asymmetric catalysis plays a key role in modern synthetic organic chemistry, with synthetic
catalysts and enzymes being the two available options. During the latter part of the last …

Our previous contribution to increasing the efficiency of directed evolution is iterative
saturation mutagenesis (ISM) as a systematic means of generating focused libraries for the …

Random mutagenesis has the potential to optimize the efficiency and selectivity of protein
catalysts without requiring detailed knowledge of protein structure; however, introducing …

Directed enzyme evolution has proven to be a powerful tool for improving a range of
properties of enzymes through consecutive rounds of diversification and selection. However …