Pires, D. E. V., Ascher, D. B. & Blundell, T. L. DUET: a server for predicting effects of mutations on protein stability using an integrated computational approach.
Acquisition of mutations is central to evolution; however, the detrimental effects of most mutations on protein folding and stability limit protein evolvability.
The ability to predict the effects of mutations on protein folding rates and mechanisms would greatly facilitate folding studies.
The effect of glycans and surface mutations on protein unfolding induced by heat or urea has been studied.
We also assess the impact of BPS mutations on protein structure and activity to elucidate the molecular origins of the disease.
The robust quantification of over 9,000 proteins and 11,000 phosphopeptides on average enabled the de novo construction of a functional protein correlation network, which ultimately exposed the collateral effects of mutations on protein complexes.
Analyzing the effect of mutations on protein stability and folding kinetics in ϕ-value analysis is commonly used to gain information about the presence of side-chain interactions in transition states.
The extinction coefficient and quantum yield of purified proteins of each construct were also examined to compare the effects of both C2 and C3 mutations on protein spectroscopic properties.
To establish the disease causality, it is necessary to investigate the effect of the mutations on protein function in further in vitro studies.
It indicates that the amount of normal protein is decreased (as seen in inborn errors of metabolism) Gain of function It refers to the functional consequences of mutations on protein function.
Tropsha now develops models to test the relation between structure and activity of drug candidates and studies protein folding and the effects of mutations on protein structure.
