Valerio Consalvi

TL;DR: The structure determination of glutamate dehydrogenase from P. furiosus contains a striking series of ion-pair networks on the surface of the protein subunits and buried at both interdomain and intersubunit interfaces, which suggest that the formation of such extended networks may represent a major stabilizing feature associated with the adaptation of enzymes to extreme temperatures.

TL;DR: From the comparative analysis of the X-ray structures available for several families of proteins, including at least one thermophilic structure in each case, it appears that thermal stabilization is accompanied by an increase in hydrogen bonds and salt bridges.

TL;DR: The purified enzyme reveals an outstanding thermal stability, totally independent of enzyme concentration, and raises questions about the roles of this enzyme in the metabolism of P. furiosus.

TL;DR: In this article, an antibody bacteriophage display library was built on the scaffold of a single-chain variable fragment (scFv) previously proven to be functionally expressed in the reducing environment of both bacterial and plant cytoplasm and endowed with intrinsic high thermodynamic stability.

TL;DR: Very high levels of glutamate dehydrogenase were found in this archaebacterium which suggests that the conversion of 2-oxoglutarate and ammonia to glutamate is of central importance to the nitrogen metabolism in this bacterium.