Which window size gives you a better signal-to-noise ratio? 7-residue window 15-residue window Under what circumstances would it be important to use a narrower window? Smaller range windows alter the sensitivity of the analysis, increasing the signal-to-noise ratio. Narrow windows permit identification of membrane-spanning regions at either end of the protein. Narrow windows allow hydropathy analysis of very small peptides that have less than 10 amino acid residue Smaller window ranges identify hydrophilic regions of the protein that are likely surface-exposed.

Which window size gives you a better signal-to-noise ratio? 7-residue window 15-residue window Under what circumstances would it be important to use a narrower window? Smaller range windows alter the sensitivity of the analysis, increasing the signal-to-noise ratio. Narrow windows permit identification of membrane-spanning regions at either end of the protein. Narrow windows allow hydropathy analysis of very small peptides that have less than 10 amino acid residue Smaller window ranges identify hydrophilic regions of the protein that are likely surface-exposed.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

One common way to determine phosphorus is by mixing 12-molybdophosphate complex with ascorbic acid to give an intense blue-colored species called molybdenum blue. The absorbance of molybdenum blue can be measured at 650 nm. A calibration graph was constructed as follow. Deduce the analytical technique used and calculate the concentration of unknown water samples analyzed which demonstrated absorbance reading of 0.269 (sample 1), 0.532 (sample 2) and 0.478 (sample 3). P calibration curve 0.8 0.6 0.4 y = 0.218x + 0.004 R2 = 0.9996 0.2 0.5 1 1.5 2 2.5 3 3.5 Concentration (ppm) Absorbance
A student weighed out 0.150 g of protein powder and dissolved it in 100 mL of water (Solution 1). The student then diluted this solution by transferring 1 mL into a 25 mL flask and diluting with water (Solution 2). Finally, 1 mL of that solution was transferred to a test tube and combined with 4 mL Bradford reagent. The absorbance of the solution in the test tube was 0.187. Assuming that the best fit linear line of the standard curve was y = 0.04144 x + 0.01521 (μ g mL), calculate the percent protein by mass in the original protein powder.
Your pH meter was improperly calibrated and reports a pH value consistently lower by 0.002 compared to the correct value. This discrepancy introduces error to your data. systematic random
Which of the following are the three main factors affecting the rate of movement of a compound on a TLC plate? 1) Site-compound affinity 2) Site-solvent affinity 3) solvent-compound affinity 4) solvent-solvent affinity 5) compound-compound affinity
Protein ABC is a heme-containing protein responsible in electron transfer in microalgae. The target protein was extracted using ammonium sulfate fractional precipitation and quantified using Bradford assay. A set of solutions with increasing concentration was prepared using 15.00 mg/mL analogous protein standard [refer to succeeding table]. Each solution was treated with 80 μL of Bradford reagent and diluted to 1.500mL. The absorbance at 595 nm of each solution was obtained and presented below. Volume of protein std, μL A595 0 0.0002 10 0.0007 25 0.0075 50 0.0165 100 0.0356 250 0.0930 500 0.1950 750 0.3010 1000 0.4175 Report the equation of the calibration curve and proof of linearity (R2 value).
If the standard addition intercept is the major source of uncertainty, find the uncertainty in the concentration of Sr in tooth enamel in parts per million. Find the 95% confidence interval for Sr in tooth enamel.
Variation in volume of extraction solvent: compound X is dissolved in 20.0 mL of solvent B. Assuming a partition coefficient of PX,AB of 5.0, calculate the percentage of X that remains in solvent B if it is extracted the following volumes of solvent A: 1.0 mL 10.0 mL 20.0 mL 100.0 mL
A student weighed out 0.150 g of protein powder and dissolved it in 100 mL of water (Solution 1). The student then diluted this solution by transferring 1 mL into a 25 mL flask and diluting with water (Solution 2). Finally, 1 mL of that solution was transferred to a test tube and combined with 4 mL Bradford reagent. The absorbance of the solution in the test tube was 0.11. Assuming that the best fit linear line of the standard curve was y = 0.04144 x + 0.01521 (μ g mL), calculate the percent protein by mass in the original protein powder.
3 a) Scatchard analysis rearranges the basic equation for protein-ligand binding to enable a linear fit of experimental data for bound to free ligand concentration ([L]bound/[L]free) as a function of bound ligand concentration ([L]bound). This enables extraction of the dissociation constant KD and the total protein concentration, [P]total, from the plot. Given the standard equation for a line, y = mx + b, where x is the abscissa and y is the ordinate, express KD in terms of the fitting parameters m and b.
Using the Hard-Sphere model of cross section, a) Calculate the total cross section of proton-proton collision by looking up the radius of a proton. b) The cross section for pp collision at the LHC with √s = 14TeV is ~0.1 barn. Compare this to what you found in part a and hypothesize what could cause the difference between them.
Asparagine and glutamine residues in proteins are deamidated in an aqueous solution to yield aspartate and glutamate, respectively, and ammonium. Proteins undergoing deamidation of one or more of their Asn or Gln groups have been detected by isoelectric focusing. Why would isoelectric focusing be effective in separating deamidated from non-deamidated protein? Compare the relative pI values of the deamidated and non-deamidated proteins.
I am stuck with deriving these two equations in the far right corner in the box. i reached this far and can't seem to understand the next step moving foward. can you please derive the two equations from eqn 1,2 and 3. These are absorbance equation used in experimental determination of 2-Naphthol excited state PKa. The purpose of the formula is to find the unknown concentration of ArOH and its conjugate base in the solution given absorbance data.