Structural stability and reversible unfolding of recombinant porcine S100A12

Quantitative proteomics analysis of early recurrence/metastasis of huge hepatocellular carcinoma following radical resection

“…S100A12 is a new member of S100 protein family (calcium binding protein family); the gene encoding S100A12 was localized on the human chromosome 1q21 [61], and is normally expressed in neutrophil granulocytes, with low expression in both lymphocytes and monocytes [50]. Its reported function involves calcium regulation and arachidonic acid metabolism in the neutrophile granulocytes [50]; it has also been reported that the expression of S100A12 was up-regulated both at mRNA and protein levels in the patients with colorectal carcinoma relative to healthy volunteers [62].…”

Chemical stability of a cold-active cellulase with high tolerance toward surfactants and chaotropic agent

“…Fitting the curve resulted in a [ U ] 1/2  = 4.5 ± 0.1 M, where [ U ] 1/2 is the urea concentration at which 50% of the enzyme exist in denatured state. Furthermore, this curve (sigmoidal-like transition) suggests that there are no detectable amounts of intermediate states present during the chemical unfolding process [17], [18]. The determined value for the free energy of unfolding, considering a two-state transition, was Δ G H20 D  = 6.4 ± 0.2 kcal mol −1 with m  = 0.85 ± 0.02 kcal mol −1  M −1 .…”

“…The fraction of denatured protein, α , was calculated from the equations [17]: $\alpha =\frac{\left(I_{\text{N}}-I_{\text{obs}}\right)}{\left(I_{\text{N}}-I_{\text{D}}\right)}$ and α  +  β  = 1, in which I obs is the fluorescence intensity obtained at a particular urea concentration, and I D and I N are the values of the fluorescence intensity characteristic of the denatured and native states, respectively. Chemical unfolding results were fit using a two-state model [17], [18]. Refolding of CelE1 (at 7.5 M urea) was done by quick dilution (1:40 fold) against the same buffer without urea and under gentle agitation.…”

Structural and dynamic characterization of the Golgi Reassembly and Stacking Protein (GRASP) in solution

“…Indeed, a pronounced decrease in the secondary structure content of CnGRASP is observed by increasing or decreasing pH values ( Figure 22D), with the maximal structural content close to the pH used in the working buffer solution. However, since this behavior is not significantly different from those observed for other well-structured proteins [158,197], changes in ±2 units from the neutral pH do not do not affect significantly the CnGRASP structure, even though this protein is membrane associated and the pH can be more acidic at the lipid/water interface [210]. The very broad CD spectra obtained at pHs 4 and 5 ( Figure 22D) reflect protein aggregation, since these pH values are close to the theoretical pI of CnGRASP (~ 4.9).…”

“…ANS is a fluorescent probe widely used in the identification of accessible hydrophobic sites in proteins [157,158]. The change in the fluorescence pattern upon increasing urea concentration reflects changes in the microenvironment of ANS from a hydrophobic medium (interior of the protein -structured) to a polar environment (exposed to the solvent after denaturation) ( Figure 15A).…”