It is important to understand how the catalytic activity of enzymes is related to their
conformational flexibility. We have studied this activity–flexibility correlation using the …

Substrate binding, product release, and likely chemical catalysis in the tryptophan
biosynthetic enzyme indole‐3‐glycerol phosphate synthase (IGPS) are dependent on the …

The β1α1 loop in the tryptophan biosynthetic enzyme indole-3-glycerol phosphate synthase
(IGPS) is important for substrate binding, product release and chemical catalysis. IGPS …

The (βα) 8-barrel enzyme indole-3-glycerol phosphate synthase (IGPS) catalyzes the
multistep transformation of 1-(o-carboxyphenylamino)-1-deoxyribulose 5-phosphate (CdRP) …

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 …

Indole-3-glycerol phosphate synthase (IGPS) catalyzes the fifth step in the biosynthesis of
tryptophan. It belongs to the large and versatile family of (βα) 8-barrel enzymes but has an …

Indole-3-glycerol phosphate synthase (IGPS) is a representative of (β/α) 8-barrel proteins—
the most common enzyme fold in nature. To better understand how the constituent amino …

Indole-3-glycerol phosphate synthase catalyzes the terminal ring closure step in tryptophan
biosynthesis. In this paper, we compare the results from molecular dynamics (MD) …

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

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