Natural proteins are often only slightly more stable in the native state than the denatured
state, and an increase in environmental temperature can easily shift the balance toward …

Structural and biochemical studies on diverse enzymes have highlighted the importance of
ligand-gated conformational changes in enzyme catalysis, where the intrinsic binding …

Sexual Selection has been studied predominantly from a functional perspective with
relatively limited investigation of the mechanistic basis of female choice. In this study, we …

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 …

Function and structure are strongly coupled in obligated oligomers such as Triosephosphate
isomerase (TIM). In animals and fungi, TIM monomers are inactive and unstable. Previously …

Ancestral sequence reconstruction has been broadly employed over the past two decades
to probe the evolutionary history of life. Many ancestral sequences are thermostable …

Triosephosphate isomerase (TPI) is a glycolysis enzyme, which catalyzes the reversible
isomerization between dihydroxyactetone-3-phosphate (DHAP) and glyceraldehyde-3 …

Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the rapid
interconversion of dihydroxyacetone phosphate (DHAP) and (R)-D-glyceraldehyde 3 …

Every quarter, The FEBS Journal presents some of its 'hidden gems'–original research and
review‐type articles that provide a significant advance or discuss recent developments in the …

Triosephosphate isomerase (TPI) is a glycolysis enzyme, which catalyzes the reversible
isomerization between dihydroxyactetone-3-phosphate (DHAP) and glyceraldehyde-3 …