Aptamers are short oligonucleotides isolated in vitro from randomized libraries that can bind
to specific molecules with high affinity, and offer a number of advantages relative to …

Improving protein stability is an important goal for basic research as well as for clinical and
industrial applications but no commonly accepted and widely used strategy for efficient …

Motivation Understanding the relationship between the sequence, structure, binding energy,
binding kinetics and binding thermodynamics of protein–protein interactions is crucial to …

Protein–protein interactions (PPIs) play a vital role in cellular functions and are essential for
therapeutic development and understanding diseases. However, current predictive tools …

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

Protein–protein interactions play a crucial role in all cellular functions and biological
processes and mutations leading to their disruption are enriched in many diseases. While a …

Predicting the structure and thermodynamics of protein–protein interactions (PPIs) are key to
a proper understanding and modulation of their function. Since experimental methods might …

Protein–protein interactions (PPIs) are vital to all biological processes. These interactions
are often dynamic, sometimes transient, typically occur over large topographically shallow …

Highlights•Reviewed scoring schemes and conformational sampling for protein–protein
complex structure prediction.•Discussed the database for binding affinity of complexes and …

The formation of protein-protein complexes is essential for proteins to perform their
physiological functions in the cell. Mutations that prevent the proper formation of the correct …