The urea-induced denaturation of dimeric Erythrina indica lectin (EIL) has been studied at pH 7.2 under equilibrium and kinetic conditions in the temperature range of 40-55 degrees C. The structure of EIL is largely unaffected in this temperature range in absence of denaturant, and also in 8 M urea after incubation for 24 h at ambient temperature. The equilibrium denaturation of EIL exhibits a ...

We explore the analytical performance and limitations of optically monitoring aqueous-phase temperature using protein-protected gold nanoclusters (AuNCs). Although not reported elsewhere, we find that these bio-passivated AuNCs show pronounced hysteresis upon thermal cycling. This unwanted behaviour can be eliminated by several strategies, including sol-gel coating and thermal denaturation of t...

The stability and compatibility of designed coiled coil peptides towards the selective incorporation of γ(4)-amino acids at the hydrophobic positions of the heptad repeat are studied. Investigations reveal that the low thermal denaturation temperature of γ(4)-residue mutated coiled coils can be utilized as a mild hyperthermia trigger in liposomes.

Botulinum neurotoxins (BoNTs) and their fragments are targets of therapeutic developments and are increasingly used as therapeutic, prophylactic, and research reagents. However, published data on their properties vary widely. In order to gain a better understanding of these variations, we initiated a systematic investigation of the stability parameters of catalytic light chains (Lc) as well as ...

The effects of high temperatures on catalytic activity and binding abilities of crude Trichoderma reesei cellulases in solution and adsorbed to a cotton fabric were studied. Above optimum temperature of 508C, catalytic activities were severely diminished but the binding behaviour was not found to be adversely affected. In order to verify possible applications of cellulases adsorbed to cotton fa...

Adapting metabolic enzymes of microorganisms to low temperature environments may require a difficult compromise between velocity and affinity. We have investigated catalytic efficiency in a key metabolic enzyme (dihydrofolate reductase) of Moritella profunda sp. nov., a strictly psychrophilic bacterium with a maximal growth rate at 2 degrees C or less. The enzyme is monomeric (Mr=18,291), 55% i...

Hydration effects on the thermal stability of glycinin (soybean 11S protein) were examined by differential scanning calorimetry (DSC). In a model system with pure glycinin, the denaturation temperature (Td) decreased with increasing moisture. Between 22 and 44% moisture, two endotherms were observed, where the lower-temperature endotherm became progressively reduced in magnitude with a concomit...

Abs t r ac t -1 . The temperature dependence of myosin ATP-ase and intestinal alkaline phosphatase from a variety of lizards having distinct preferred temperatures was compared. 2. The ATP-ase was relatively thermolabile; reductions in activity at temperatures above the optimum resulted primarily from irreversible denaturation. However, pronounced differences were evident in both the optimal te...

Single domain antibodies are the small recombinant variable domains derived from camelid heavy-chain-only antibodies. They are renowned for their stability, in large part due to their ability to refold following thermal or chemical denaturation. In addition to refolding after heat denaturation, A3, a high affinity anti-Staphylococcal Enterotoxin B single domain antibody, possesses a melting tem...