d Table FO From Picture B Pictures Shapes Icons ✓ fx [3H]-spiperone M C ZV F O V 1.4 1.2 1 0.8 0.6 0.4 0.2 D .... 0 0.00E+00 My Add-ins ✓ · F 2.00E-10 Recommended Charts 4.00E-10 total binding pmol/mg E Chart Title ✓✓ Maps 8.00E-10 6.00E-10 Non Specific binding pmol/mg F Pivot Chart G 1.20E-09 1.00E-09 Specific binding pmol/mg Sparklines H 1.406-09 Timeline 1 Link Forr > Fill > Line
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hi can you find the maximum binding capacity(b max) using the table
Step by step
Solved in 3 steps
is this the same as the Bmax because i need to find the bmax
- What is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM. 0.01 B.0.1 C.0.91 D.0.99 none of the listed valuesq44 please calculate the unknown concentration of the protein A wih an absorbance value of A188 given the standard curve indicated in the table. write your answers in numbers only with 2 decimals. protein concentration (ug/ml) absorbance 0 0.000 0.02 0.161 0.04 0.284 0.06 0.438 0.08 0.572 0.10 0.76280mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCL needed to reach relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
- Rx Of oxacinophtalmic solution 3% Disp. 10 mL How many milligrams of axacin contained in each milliter of the dispensed prescription?Thesecondarystructureofaproteinisinfluencedbybothhydrogen bonding and London dispersion forces. a. Usingastructuralformula,showanexampleofhydrogenbonding between the serine portion of a protein and the tyrosine portion b. Usingastructuralformula,showanexampleofLondondispersionforces between the leucine portion of a protein and the valine portion1. AsnIleGlyTyrGluProSerArgAsp 2. MetPheAsnSerGluProLysCys 3. SerArgGluTyrValValThrPheGly 4. MetPheSerThrAspGluVal
- A 0.0284 M aqueous solution of lactic acid, HC3H5O3, a substance that accumulates in the blood and muscles during physical activity, is found to be 6.7% ionized. Determine the value of Ka for lactic acid.You have a mixture of 4 amino acids (Q, W, E, R, T) that you want to separate using ion exchange chromatography. Which of these amino acids would bind most strongly to a DEAE anion exchange column at pH 7? Q W E R Tɡive me example about the arranɡements of heptapeptide such as Arɡ, Phe, Val and etc.
- Which method of chromatography would be the most appropriate for separating mixtures of thefollowing peptides at a neutral pH? (a) ARDDEKLLML, LMYWWILLDETSARALIV, DQNNA(b) GATSKKIVLM, ASCILLVMEN, MFDDAAYVNE(c) KLMDAATSPFLMAGHHHHHH, MFPSATEKRQQNNESTVLAG In what order would the following peptides be eluted from an anion exchange column at pH 7.5?Peptide 1: Ala–Asp–Glu–Gln–Trp–Leu–His–ValPeptide 3: Phe–Gln–Glu–Ala–Gln–His–Leu–Arg-IlePeptide 2: Arg–Ile–Pro–Lys–Cys–Met–LysA stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?a drug is order 100mg/m2 po BID. How many milliliters will a patient receive if her BSA is 1.80m2 and concentration of solutions is 100mg/5ml?