The stability and activity of indole-3-glycerol phosphate synthase from Sulfolobus
solfataricus were studied as a function of pH and temperature. In this paper we focus on …

As a test of the hypothesis that folding mechanisms are better conserved than sequences in
TIM barrels, the equilibrium and kinetic folding mechanisms of indole-3-glycerol phosphate …

Abstract Indole-3-glycerol-phosphate synthase, a thermophilic and thermostable enzyme
from the archaeon Sulfolobus solfataricus, was purified and characterized. The sequence of …

The structures of partially folded states appearing during the folding of a (βα) 8 TIM barrel
protein, the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus (sIGPS), was …

To test the roles of motif and amino acid sequence in the folding mechanisms of TIM barrel
proteins, hydrogen-deuterium exchange was used to explore the structure of the stable …

The recombinantly expressed protein indoleglycerol phosphate synthase from the
hyperthermophilic bacterium Thermotoga maritima (tIGPS) was purified and characterized …

The role of the extra helix α0 in the N-terminal extension of the eight-fold βα barrel of
indoleglycerol phosphate synthase was probed by point mutation and truncation. Replacing …

The crystal structure of the thermostable indoleglycerol-phosphate synthase from
Thermotoga maritima (tIGPS) was determined at 2.5 Å resolution. It was compared with the …

Indole-3-glycerol phosphate synthase from the hyperthermophilic ar chaeonSulfolobus
solfataricusis a monomeric enzyme with the common (β/α) 8-fold. Recently, its three …

Background: Recent efforts to understand the basis of protein stability have focussed
attention on comparative studies of proteins from hyperthermophilic and mesophilic …