Natural metalloproteins perform many functions—ranging from sensing to electron transfer
and catalysis—in which the position and property of each ligand and metal are dictated by …

A grand challenge in the field of structural biology is to design and engineer proteins that
exhibit targeted functions. Although much success on this front has been achieved, design …

Computationally modeling changes in binding free energies upon mutation (interface ΔΔ G)
allows large-scale prediction and perturbation of protein–protein interactions. Additionally …

Natural enzymes are delicate biomolecules possessing only marginal thermodynamic
stability. Poorly stable, misfolded, and aggregated proteins lead to huge economic losses in …

Accurately predicting changes in protein stability upon amino acid substitution is a much
sought after goal. Destabilizing mutations are often implicated in disease, whereas …

Highlights•Laboratory directed evolution and ancestral reconstruction can facilitate study of
protein structural dynamics.•Advances in biophysical and computational techniques facilitate …

Engineered proteins, especially enzymes, are now commonly used in many industries
owing to their catalytic power, specific binding of ligands, and properties as materials and …

Proteins are intrinsically dynamic molecules that can exchange between multiple
conformational states, enabling them to carry out complex molecular processes with extreme …

Computational structure-based protein design programs are becoming an increasingly
important tool in molecular biology. These programs compute protein sequences that are …

Motivation The ABACUS (ab ackbone-based a mino ac id u sage s urvey) method uses
unique statistical energy functions to carry out protein sequence design. Although some of …