Polyprotic acids such as H3PO4, can act as acid-base buffers ℗ only in combination with polyprotic bases Ⓡ if their concentration is kept low at pH values around neutrality
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- At what pH does a lysine solution exhibit the highest buffering capacity? (Lysine pKas: pk1 = 2.2, pK2 = 8.95, pK3 = 10.5) %3D O рH 12.1 О рH 9.72 O pH 5.67 pH 8.957. · In the space provided, sketch a titration curve (pH vs H+ ions dissociated) of a phosphate buffer shown below. The pKa of H2PO4 is 7.0. H,PO, НРО, + 9. 8. 7 pH 3 1.0 0.5 H+ dissociated --> b. What is the effective buffering range of this acid? At what pH will you have 25% of the buffer in the form of H2PO4? с.10 tab of acetaminophen 500 mg molar absorptivity= 14520 @ 243nm. The total weight of the 10tab is 5278 mg. I take a sample equivalent to 100mg of tablet and I diluted it in 100mL, I took an aliquot of 10mL and I diluted it in 250mL, of these I took 25mL and I diluted them in 250mL. Calculate the weight per tablet. Absorbance = 0.944
- determine the pKa of the acid and ph of the buffer sol'n of a buffer mixed with 0.1 M tris and 0.5 M chloine salt having dissociation constant of 1.072x10^-6.CAR) All una Red stock soluton concentration: wis strue Somple #yelume dilution 1 ete total tock AR volume 50.00m 50. 00mL 50.00L AR COC conentrastion Absorbance Q dilutibn 2 dilution 3 10 O. 16.4 20 0. 237 turn dilution 4 25 So00 O. 392 shift unknarn 1 0.485 (Include a printed copy of the colibratlon curve) Colibrotion urve cayotion: R2 valveThe ideal buffer range for any amino acids is pH above or below its pI values because the amino acid will get get precipitated at its pI. pKa1 of -COOH group of Cys = 1.71 pKa2 of -NH2 group of Cys = 10.78 pKa3 of side chain group of Cys = 8.33 (it indicates that the thiol group of Cys is a strong acid than the -NH2 group pf Cys as pKa Cys side chain is lower). Thiol side chain of Cys will loose proton first than -NH2. Net charge on Cys is zero in structure B, i.e. Structure B is a zwitterion and pI can be calculated from pKa1 and pKa3. Structure B of Cys, pI = (8.33 + 1.71) / 2 = 10.04/2 = 5.02 pH above its pI the Cys will be -vely charged (deprotonated) while pH below its pI it will be +vely charged (protonated). So, selection of buffer depends on its pI values, not pKa values of each functional group, QUESTION: What are the buffer regions/effective pH range?
- An appropriate biochemical buffer should have charges in both its conjugate acid and conjugate base form. This avoids the presence of a neutral form of the buffer that might be able slowly leak into cells. Does unmodified dimethylpiperazine meet this criterion when buffering at pH 8? O Yes No What about buffering at pH 4? D Yes NoWhich of the following is TRUE if pH is higher than the pka of the buffer? O [weak acid] approximately 0 O [conjugate base] = [weak acid] [conjugate base] > [weak acid] O [conjugate base] < [weak acid]What phosphate buffer conditions can be used to isolate protein (isoelectric point of 5.2) using anion exchanger? Using Henderson Hasselbach equation, show this buffer is made inluding calculations
- A large chaperone protein complex GroEL is approximately 16 nm in diameter. When it is dissolved in water at 300 K, estimate the average time it will take for GroEL to diffuse a distance of 500 nm (0.5 micron). The viscosity of water is 10-3 Pa*s.Calculate the volume of TAE buffer that you will need to prepare a 100ml solution of 1X strength if you only have a 50X concentrated solution available.A 100 ml of a 1% sol'n of boric acid (freezing point = -0.29) isotonic w/ blood by NaCl (freezing point = -0.58). what grams is needed to make it an isotonic? what weight of NaCl is needed to a 2% sol'n of atropine sulfate (E=0.13) made isotonic with blood plasma?