Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

Enzymes generated by natural recruitment and protein engineering have greatly contribute
in various sets of applications. However, their insufficient stability is a bottleneck that limit the …

Computational methods that predict protein stability changes induced by missense
mutations have made a lot of progress over the past decades. Most of the available methods …

Rotamer libraries are used in protein structure determination, prediction, and design. The
backbone-dependent rotamer library consists of rotamer frequencies, mean dihedral angles …

The ability of proteins to establish highly selective interactions with a variety of (macro)
molecular partners is a crucial prerequisite to the realization of their biological functions. The …

Naturally occurring IgG antibodies are bivalent and monospecific. Bispecific antibodies
having binding specificities for two different antigens can be produced using recombinant …

Stability is a fundamental property affecting function, activity, and regulation of biomolecules.
Stability changes are often found for mutated proteins involved in diseases. Stability …

While nature evolved polypeptides over billions of years, protein design by evolutionary
mimicry is progressing at a far more rapid pace. The mutation, selection, and amplification …

Methods for protein modeling and design advanced rapidly in recent years. At the heart of
these computational methods is an energy function that calculates the free energy of the …

Software to predict the change in protein stability upon point mutation is a valuable tool for a
number of biotechnological and scientific problems. To facilitate the development of such …