The principles of isothermal titration calorimetry (ITC) and differential scanning calorimetry
(DSC) are reviewed together with the basic thermodynamic formalism on which the two …

Recent data have highlighted the enigmatic role that water plays in biomolecular complexes.
Water at the interface of a complex can increase the promiscuity of an interaction, yet it can …

The stability of proteins in aqueous solution is routinely enhanced by cosolvents such as
glycerol. Glycerol is known to shift the native protein ensemble to more compact states …

The understanding of molecular recognition processes of small ligands and biological
macromolecules requires a complete characterization of the binding energetics and …

Many anticancer, antibiotic, and antiviral drugs exert their primary biological effects by
reversibly interacting with nucleic acids. Therefore, these biomolecules represent a major …

Adeno-associated viruses (AAV) are ubiquitous in the human population (> 90% of adults
are seropositive) but have never been implicated as the cause of any disease. They were …

With the numerous detailed molecular descriptions of antibody-antigen interfaces, the
structural study of these molecular interactions has evolved from an attempt to understand …

Yeast surface display is a eucaryotic system for the directed evolution of protein binding and
stability. For antibody affinity maturation, achievable single‐pass enrichment factors are a …

Many cellular functions rely on interactions between protein pairs and higher oligomers. We
have recently shown that binding mechanisms are robust and owing to the minimal …

Publisher Summary This chapter discusses that isothermal titration calorimetry (ITC) follows
the heat change when a test compound binds to a target protein. It allows precise …