originpro8  (OriginLab)

Journal: ACS applied materials & interfaces

Article Title: Electrochemical quantification of glycated and non-glycated human serum albumin in synthetic urine

doi: 10.1021/acsami.8b16071

Figure Lengend Snippet: Preparation of the biosensor for measurements. (a) Electrical contacts to the prepared devices are made with copper tape, platinum foil (as the counter electrode) and alligator pins. (b) Measurements were performed using a PalmSens3 analyzer controlled by PS-Trace 4.8. Data was processed with GNU Octave, Igor Pro, and OriginLab Pro 8.

Article Snippet: All electrochemical data was processed on GNU Octave, Igor Pro and OriginLab Pro 8 software.

Techniques:

Journal: PLoS ONE

Article Title: Inactivation of the Antibacterial and Cytotoxic Properties of Silver Ions by Biologically Relevant Compounds

doi: 10.1371/journal.pone.0094409

Figure Lengend Snippet: The cytotoxicity of silver nitrate to human skin cells. Viability of primary adult human dermal fibroblasts exposed to AgNO 3 for 4 h or 24 h in (A) Medium 106; (B) Medium 106+1 mmol dm −3 GSH. Sigmoidal curves were fitted using the Boltzman function in OriginPro8 (OriginLab). Error bars = SEM, n = 4. GSH, reduced glutathione.

Article Snippet: The optical density of each individual culture at 16 hr or 24 hr was plotted in OriginPro8 (OriginLab) and Sigmoidal curves fitted using the Boltzman function.

Techniques:

Journal: PLoS ONE

Article Title: Differential thermal stability, conformational stability and unfolding behavior of Eis proteins from Mycobacterium smegmatis and Mycobacterium tuberculosis

doi: 10.1371/journal.pone.0213933

Figure Lengend Snippet: Unfolding and refolding kinetics of MsEis protein. Intrinsic tryptophan fluorescence spectra of either unfolded or refolded MsEis protein in the presence or absence of GdmCl and urea at different time intervals. 0 h (Panel A) , 2 h (Panel B) , 4 h (panel C) , 6 h (Panel D) , 8 h (Panel E) , 10 h (Panel F) and 12 h (Panel G) . The values corresponding to native MsEis without treatment were considered as 100% in each case of unfolding or refolding. The values obtained from emission maxima were fitted using OriginPro 8.0 software.

Article Snippet: The obtained data points were fitted to three-state model (biDose-response curve of nonlinear regression analysis) using OriginPro 8 software (Origin Lab, Northampton, USA).

Techniques: Fluorescence, Software

Journal: PLoS ONE

Article Title: Differential thermal stability, conformational stability and unfolding behavior of Eis proteins from Mycobacterium smegmatis and Mycobacterium tuberculosis

doi: 10.1371/journal.pone.0213933

Figure Lengend Snippet: Time kinetics, temperature stability and steady-state kinetic parameters of KAN acetylation by MsEis and RvEis. Time course of changes in the absorbance at 412 nm of NTB - ions formed as a result of acetyltransferase activity of MsEis and RvEis proteins (Panel A) . The effect of temperature on the catalytic activity of MsEis and RvEis was determined after incubating the Eis proteins at different temperatures ranging from 20°C to 80°C (Panel B) . Kinetic parameters were calculated for the acetylation of KAN by MsEis and RvEis at fixed concentration of acetyl CoA and increasing concentration of KAN antibiotic (Panel C) . The experimental values were fitted to Michaelis-Menten equation using OriginPro 8.0 software (Origin Labs, Northampton, USA).

Article Snippet: The obtained data points were fitted to three-state model (biDose-response curve of nonlinear regression analysis) using OriginPro 8 software (Origin Lab, Northampton, USA).

Techniques: Activity Assay, Impedance Spectroscopy, Concentration Assay, Software

Journal: PLoS ONE

Article Title: Differential thermal stability, conformational stability and unfolding behavior of Eis proteins from Mycobacterium smegmatis and Mycobacterium tuberculosis

doi: 10.1371/journal.pone.0213933

Figure Lengend Snippet: Comparison of conformational stability of MsEis and RvEis proteins in the presence of different denaturants. Intrinsic tryptophan fluorescence spectra of MsEis and RvEis proteins in the presence of increasing concentration of GdmCl (Panel A), urea (Panel C) and at increasing temperature from 25°C to 100°C (Panel E) . Unfolding of MsEis and RvEis proteins measured in terms of changes in emission wavelength maxima in the presence of GdmCl (Panel B), urea (panel D) and temperature (Panel F) . The values corresponding to native Eis without treatment were considered as 100%. Fitting of the values obtained from emission maxima were done by using equations with OriginPro 8.0 software.

Article Snippet: The obtained data points were fitted to three-state model (biDose-response curve of nonlinear regression analysis) using OriginPro 8 software (Origin Lab, Northampton, USA).

Techniques: Fluorescence, Concentration Assay, Impedance Spectroscopy, Software

Journal: Neurobiology of aging

Article Title: Amyloid beta and the longest-lived rodent: the naked mole-rat as a model for natural protection from Alzheimer’s disease

doi: 10.1016/j.neurobiolaging.2013.03.032

Figure Lengend Snippet: Grain analysis data reveal that aggregation properties depend on sequence and incubation conditions. Grain analysis data extracted from 3 fields for both human and NMR Aβ 1–42 examined with AFM OriginPro 8.6 (OriginLab Corp., Northampton,

Article Snippet: Grain analysis data collected from 3 0.49 µm2 or 1 µm2 fields in each case was further examined with OriginPro 8.6 (OriginLab Corp, Northampton, MA).

Techniques: Sequencing, Incubation, Nuclear Magnetic Resonance