In the early 2000s, Tawfik presented his 'New View'on enzyme evolution, highlighting the
role of conformational plasticity in expanding the functional diversity of limited repertoires of …

Function in biological systems is exquisitely dependent on spatial and temporal changes in
biomacromolecules. Innumerable biological processes ultimately rely on transduction of …

A unique feature of chemical catalysis mediated by enzymes is that the catalytically reactive
atoms are embedded within a folded protein. Although current understanding of enzyme …

Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme
motions linked to substrate turnover remain largely unknown. We have studied dynamics of …

Enzymes are very efficient catalysts that are essential for the functioning of living organisms.
The low efficiency of biocatalysts produced de novo relative to those that have evolved …

Enzyme catalysis is an inherently dynamic process. Binding and release of ligands is often
accompanied by conformational changes, both subtle and dramatic (reviewed more …

▪ Abstract We describe large scale ab initio quantum chemical and mixed quantum
mechanics/molecular mechanics (QM/MM) methods for studying enzymatic reactions. First …

A fundamental question is how enzymes can accelerate chemical reactions. Catalysis is not
only defined by actual chemical steps, but also by enzyme structure and dynamics. To …

While traditional 1H, 13C, and 15N (HCN) solution state NMR protocols provide a wealth of
data on protein structure and dynamics, 19F NMR provides a unique perspective of …

Site-directed spin labeling is a general method for investigating structure and conformational
switching in soluble and membrane proteins. It will also be an important tool for exploring …