at is the wavelength of maximum aborbance for the Bradford reagent in its blue form. at is the wavelength of maximum aborbance for the Bradford reagent in its red form. at is the wavelength of maximum sensitivity for the spectrophotometer. doesn't really matter. Any wavelength would work fine.
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- If you mix two unknown samples and repeat the Lowry assay, is the absorbance equivalent to the sum of the two individual unknown samples that is used.After performing the manual Albumin assay, you get the absorbance value of 0.205 for a 4.5 g/dL albumin standard and 0.114 for control A. What is the calculated value of the control? (just write a number with one decimal, the units will be mg/dL)Voges Proskauer test Does color of the medium change to red after both reagents were added and allowed to sit for 60 minutes? If yes, after about how many minutes before you can see red color?
- In the ELISA, the pH the coating buffer was 9.6 whereas the pH of the sample buffer (PBS based) was 7.4 a) Why was the pH of the coating buffer so different?b) What is “coating buffer” for an ELISA? Does the buffer molecule usedmake sense based on the desired pH?In an ELISA procedure the samples are incubated and the ELISA plate iscovered with parafilm and placed in a humidified chamber to preventevaporation of the small liquid volumes in the wells.c) How would your results change if you did not incubate in a humidifiedchamber?Briefly explain how you could use the color of the Coomassie assay sample solution to determine if anunknown sample needs to be diluted in order to measure the sample’s concentrationAfter adding stop solution (sulphuric acid) in reaction mixture of HRP assay with TMB, yellow color becomes brighter. What is the mechanism?
- How could you utilize fluorescence quenching in the different analytical application? Please answer shorty at your own words. Answer should be to the point.In your opinion, for efficient multiphoton excited fluorescence microscopy, would it be better to use a 100 fs 80 MHz laser pulse train or a 200 fs 80 MHz laser pulse train for imaging biological samples? Please explain your answer using equations 1 and 2 <I(t)2> = gP <I(t)>2 / (Rτ) ..............equa (1) τout = τin (1 + 7.68(D/τ2in)2) 1⁄2 ................equa (2) D is the total dispersion in femtoseconds squared gp is a unitless factor that depends on the temporal laser pulse shape (0.66 for a Gaussian pulse shape), τ is the full-width half-maximum (FWHM) of time average valuePlease answer fast What are some similarities and differences in Bradford assay and Nanodrop (to obtain direct absorbance measurements). What are the benefits and setbacks of them. How is 260/280 absorbance ratio significant?
- When run under nondenaturing conditions (without SDS or β-mercaptoethanol), nativepolyacrylamide gel electrophoresis (PAGE) allows proteins to maintain biological activity, so the GFP band should fluoresce when exposed to UV light. How do the staining patterns of gels run in this way differ from the staining patterns of gels run using SDS-PAGE?Why is control of column and detector temperature more important for non- suppressed IC (Ion Chromatography) than it is for suppressed IC?When bound to proteins, the Bradford reagent turns blue. You measured the absorbance of your samples at 595 nm, which corresponds to yellow light. Why did you measure the absorbance using yellow light instead of blue light?