peak fitting module of origin 8.1 (OriginLab corp)
OriginLab corp manufactures this product 
90
Structured Review
OriginLab corp
peak fitting module of origin 8.1
Peak Fitting Module Of Origin 8.1, supplied by OriginLab corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/origin+peak-fitting+module/peak+fitting+software+origin+version+7+5/pmc11943184-280-5-7
Average 90 stars, based on 1 article reviews
Peak Fitting Module Of Origin 8.1, supplied by OriginLab corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/origin+peak-fitting+module/peak+fitting+software+origin+version+7+5/pmc11943184-280-5-7
Average 90 stars, based on 1 article reviews
peak fitting module of origin 8.1 - by Bioz Stars,
2026-10
90/100 stars
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other:Article Title: Binding of Ca2+ and Zn2+ to factor IX/X-binding protein from venom of Agkistrodon halys Pallas: stabilization of the structure during GdnHCl-induced and thermally induced denaturation. Article Snippet: Coagulation factor IX/coagulation factor X binding protein from the venom of Agkistrodon halys Pallas (AHP IX/X-bp) is a unique coagulation factor IX/coagulation factor X binding protein (IX/X-bp).. Among all IX/Xbps identified, only AHP IX/X-bp is a Caand Znbinding protein.. The binding properties of Ca and Zn ions binding to apo-AHP IX/X-bp and their effects on the stability of the protein have been investigated by isothermal titration calorimetry, fluorescence spectroscopy, and differential scanning calorimetry. Article Title: Differential scanning calorimetric, circular dichroism, and Fourier transform infrared spectroscopic characterization of the thermal unfolding of xylanase A from Streptomyces lividans. Article Snippet: The thermal unfolding of xylanase A from Streptomyces lividans, and of its isolated substrate binding and catalytic domains, was studied by differential scanning calorimetry and Fourier transform infrared and circular dichroism spectroscopy.. Our calorimetric studies show that the thermal denaturation of the intact enzyme is a complex process consisting of two endothermic events centered near 57 and 64°C and an exothermic event centered near 75°C, all of which overlap slightly on the temperature scale.. A comparison of the data obtained with the intact enzyme and isolated substrate binding and catalytic domains indicate that the lowerand higher-temperature endothermic events are attributable to the thermal unfolding of the xylan binding and catalytic domains, respectively, whereas the higher-temperature exothermic event arises from the aggregation and precipitation of the denatured catalytic domain. |