A survey of protein databases indicates that the majority of enzymes exist in oligomeric
forms, with about half of those found in the UniProt database being homodimeric …

The moderate stability of enzymes is one of the main drawbacks that hinder general
implementation of these interesting biocatalysts at industrial scale. An especially complex …

The computer-based design of protein–protein interactions is a rigorous test of our
understanding of molecular recognition and an attractive approach for creating novel tools …

Dextran aldehyde (dexOx), resulting from the periodate oxidative cleavage of 1, 2-diol
moiety inside dextran, is a polymer that is very useful in many areas, including as a …

The enzyme glutamate dehydrogenase (GDH) from Escherichia coli is a hexameric protein.
The stability of this enzyme was increased in the presence of Li+ in concentrations ranging …

Triosephosphate isomerase (TIM) is a ubiquitous enzyme, which appeared early in
evolution. TIM is responsible for obtaining net ATP from glycolysis and producing an extra …

Triosephosphate isomerase (TPI) is a glycolytic enzyme which homodimerizes for full
catalytic activity. Mutations of the TPI gene elicit a disease known as TPI Deficiency, a …

The design of proteins with tailored functions is of immense interest to biotechnology,
medicine, and the chemical industry. While protein design is rapidly evolving with the use of …

The dimeric nature of triosephosphate isomerases (TIMs) is maintained by an extensive
surface area interface of more than 1600 Å2. TIMs from Trichomonas vaginalis (TvTIM) are …

Function, structure, and stability are strongly coupled in obligated oligomers, such as
triosephosphate isomerase (TIM). However, little is known about how this coupling evolved …