Psychrophilic, mesophilic, and thermophilic alpha-amylases have been studied as regards their conformational stability, heat inactivation, irreversible unfolding, activation parameters of the reaction, properties of the enzyme in complex with a transition state analog, and structural permeability. These data allowed us to propose an energy landscape for a family of extremophilic enzymes based o...

Three polypropylene samples (1-3) were synthesized with a 4th generation Ziegler-Natta catalyst in the presence of cyclohexyldimethoxymethylsilane (donor c), dicyclopenthyldimethoxysilane (donor d) and diisopropyldimethoxysilane (donor p), respectively, as external electron donors. The physical properties of the synthesized polypropylenes were determined. For samples 1 to 3, Successive self-nuc...

Now that enzymes are available that are stable above 100 degrees C it is possible to investigate conformational stability at this temperature, and also the effect of high-temperature degradative reactions in functioning enzymes and the inter-relationship between degradation and denaturation. The conformational stability of proteins depends upon stabilizing forces arising from a large number of ...

Caseinolytic proteases are large oligomeric assemblies responsible for maintaining protein homeostasis in bacteria and in so doing influence a wide range of biological processes. The functional assembly involves three chaperones together with the oligomeric caseinolytic protease catalytic subunit P (ClpP). This protease represents a potential target for therapeutic intervention in pathogenic ba...

In recent years the issues of protein stability, folding and aggregation have become central in several pathological conditions and in particular in amyloid diseases. Here, we review the recent developments on the molecular mechanisms of amyloid formation by transthyretin (TTR), in particular, in what concerns to protein conformational stability, protein folding and

The two most common methods of measuring the conformational stability of a protein are differential scanning calorimetry and an analysis of solvent denaturation curves by using the linear extrapolation method. In this article, we trace the history of the linear extrapolation method, review how the method is used to measure protein stability, and then discuss some of the other important uses.

Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis in order to determine whether it can be dissociated into monomers. Two hTIM mutants were produced, in which a glutamine residue was substituted for either Met14 or Arg98, both of which are interface residuces. These substitutions strongly interfere with TIM subunit association, since these mutant ...

hybrid-density functional theory (b3lyp/def2-tzvpp) based method and nbointerpretation were used to investigate the conformational behavior of 1,2-dihalodisilanes[halo=f (1), cl (2), br (3), i (4)]. the b3lyp/def2-tzvpp results showed that the anticonformations of compounds 1-4 are more stable than their corresponding gaucheconformations. the stability of the anti conformation compared to the g...